Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain

As a secondary messenger, calcium participates in various physiological and biochemical reactions in plants. Photosynthesis is the most extensive biosynthesis process on Earth. To date, researchers have found that some chloroplast proteins have Ca2+-binding sites, and the structure and function of some of these proteins have been discussed in detail. Although the roles of Ca2+ signal transduction related to photosynthesis have been discussed, the relationship between calcium and photosynthesis is seldom systematically summarized. In this review, we provide an overview of current knowledge of calcium’s role in photosynthesis.

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Quinol binding sites and ubisemiquinone stabilisation in the Escherichia coli quinol oxidase, cytochrome bo3. A discussion of models for structure and function

Biochemical Society Transactions ◽

10.1042/bst027a081c ◽

1999 ◽

Vol 27 (3) ◽

pp. A81-A81

Author(s):

W. John Ingledew ◽

Lewis Murray ◽

Ricardo H. Pires

Keyword(s):

Escherichia Coli ◽

Binding Sites ◽

Structure And Function ◽

Quinol Oxidase ◽

Cytochrome Bo3 ◽

Quinol Binding ◽

And Function

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Multiple Ca2+ Binding Sites in the RCK Domain Contribute to Gating in the MthK K+ Channel

Biophysical Journal ◽

10.1016/j.bpj.2011.11.3746 ◽

2012 ◽

Vol 102 (3) ◽

pp. 690a

Author(s):

Frank J. Smith ◽

Victor P.T. Pau ◽

Alexander B. Taylor ◽

Liubov V. Parfenova ◽

Elsie Samakai ◽

...

Keyword(s):

Binding Sites ◽

K Channel ◽

Rck Domain

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Effect of cross-linkers on the structure and function of pig-renal sodium–glucose cotransporters after papain treatment

Biochemical Journal ◽

10.1042/bj3300733 ◽

1998 ◽

Vol 330 (2) ◽

pp. 733-736 ◽

Cited By ~ 2

Author(s):

Jean GIUDICELLI ◽

Marie-France BERTRAND ◽

Stephane BILSKI ◽

T. Than TRAN ◽

Jean-Claude POIREE

Keyword(s):

Binding Sites ◽

Specific Inhibitor ◽

Structure And Function ◽

Scatchard Analysis ◽

High Affinity ◽

Phlorizin Binding ◽

Sodium Dependent ◽

Spacer Arm ◽

Molecular Masses ◽

And Function

Kidney brush-border membranes contain two sodium-dependent glucose transporters, one with low and one with high affinity for phlorizin, the specific inhibitor of these transporters. Using Scatchard analysis of phlorizin binding and Western blotting with specific antibodies against these transporters, we demonstrate in this study that although both transporters were proteolysed by papain treatment, only the high-affinity phlorizin-binding sites were decreased. Papain treatment followed by cross-linking with homobifunctional disuccinimidyl tartarate restored only the structure of the low-affinity phlorizin-binding protein (approx. molecular mass 70 kDa) without modifying the phlorizin-binding sites. When disuccinimidyl tartarate was replaced with dithiobis(succinimidyl acetate), another homobifunctional cross-linker with a higher spacer arm, the low- and high-affinity sites were both restored, with reappearance of two phlorizin-binding proteins with approx. molecular masses of 70 and 120 kDa. We conclude that high-affinity phlorizin-binding sites depend on the presence of the heterodimeric 120 kDa protein.

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Gating currents from a delayed rectifier K+ channel with altered pore structure and function

Biophysical Journal ◽

10.1016/s0006-3495(92)81770-8 ◽

1992 ◽

Vol 62 (1) ◽

pp. 34-36 ◽

Cited By ~ 12

Author(s):

M. Taglialatela ◽

G.E. Kirsch ◽

A.M. VanDongen ◽

J.A. Drewe ◽

H.A. Hartmann ◽

...

Keyword(s):

Pore Structure ◽

Structure And Function ◽

K Channel ◽

Delayed Rectifier ◽

Gating Currents ◽

And Function

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Filopodome mapping identifies p130Cas as a mechanosensitive regulator of filopodia stability

10.1101/377879 ◽

2018 ◽

Author(s):

Guillaume Jacquemet ◽

Rafael Saup ◽

Hellyeh Hamidi ◽

Mitro Miihkinen ◽

Johanna Ivaska

Keyword(s):

Binding Sites ◽

Focal Adhesions ◽

Structure And Function ◽

Structured Illumination ◽

Structured Illumination Microscopy ◽

Cell Adhesion And Migration ◽

And Migration ◽

Cellular Behaviour ◽

And Function ◽

Fine Tune

AbstractFilopodia are adhesive cellular protrusions specialised in the detection of extracellular matrix (ECM)-derived cues. While ECM engagement at focal adhesions is known to trigger the recruitment of hundreds of proteins (“adhesome”) to fine-tune cellular behaviour, the components of the filopodia adhesions remain undefined. Here, we performed a structured illumination microscopy-based screen to map the localisation of 80 target proteins, linked to cell adhesion and migration, within filopodia. We demonstrate preferential enrichment of several adhesion proteins to either filopodia tips, filopodia shafts, or shaft subdomains suggesting divergent, spatially restricted functions for these proteins. Moreover, proteins with phospho-inositide (PI) binding sites are particularly enriched in filopodia. This, together with the strong localisation of PI(3,4)P2 in filopodia tips, predicts critical roles for PIs in regulating filopodia ultra-structure and function. Our mapping further reveals that filopodia adhesions consist of a unique set of proteins, the filopodome, that are distinct from classical nascent adhesions, focal adhesions and fibrillar adhesions. Using live imaging, we observe that filopodia adhesions can give rise to nascent adhesions, which, in turn, form focal adhesions. Finally, we demonstrate that p130Cas (BCAR1) is recruited to filopodia tips via its CCHD domain and acts as a mechanosensitive regulator of filopodia stability.

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Identification and Computational Analysis of 3D-Structure Of MOCS1

10.21203/rs.3.rs-473901/v1 ◽

2021 ◽

Author(s):

Maham Hamid ◽

uzma habib ◽

Javeria Batool ◽

Arshemah Qaisar ◽

Rehan Zafar Paracha

Keyword(s):

Binding Sites ◽

Biosynthetic Pathway ◽

Computational Analysis ◽

Tertiary Structure ◽

3D Structure ◽

Structure And Function ◽

Molybdenum Cofactor ◽

Recognition Method ◽

And Function ◽

Ramachandran Plots

Abstract Cyclic pyranopterin monophosphate (cPMP) is one of the most stable intermediates in Molybdenum cofactor (MoCo) biosynthetic pathway. In humans, synthesis of cPMP from Guanosine triphosphate (GTP) requires functional genes i.e. Molybdenum Cofactor Synthesis-1 (MOCS1) genes that contains for two catalytic proteins MOCS1A and MOCS1B. Importance of MOCS1A and MOCS1B for biosynthesis of MoCo reveals from the fact that its deficiency leads to MoCo type A deficiency. As there is no structure available for MOCS1 genes in the literature, tertiary structure of MOCS1 genes were investigated in this research via threading or folds recognition method by i-TASSER and validation was done using ERRAT, Verify3D and Ramachandran plots. Binding sites were predicted and validated. Docking of MOCS1A with GTP and MOCS1B with 3, 8 dihydroguanosine was done using Autodock via PyRx. Apart from this, highly confident mutations were also predicted using SIFT and polyphen2 that can alter the structure and function of MOCS1 gene.

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Structural and mechanistic studies on the peroxisomal oxygenase phytanoyl-CoA 2-hydroxylase (PhyH)

Biochemical Society Transactions ◽

10.1042/bst0350870 ◽

2007 ◽

Vol 35 (5) ◽

pp. 870-875 ◽

Cited By ~ 13

Author(s):

C.J. Schofield ◽

M.A. McDonough

Keyword(s):

Binding Sites ◽

Point Mutations ◽

Clinical Importance ◽

Structure And Function ◽

Side Chain ◽

Mechanistic Studies ◽

Pristanic Acid ◽

Methyl Group ◽

Refsum's Disease ◽

And Function

Phytanic acid (PA) is an epimeric metabolite of the isoprenoid side chain of chlorophyll. Owing to the presence of its epimeric β-methyl group, PA cannot be metabolized by β-oxidation. Instead, it is metabolized in peroxisomes via α-oxidation to give pristanic acid, which is then oxidized by β-oxidation. PhyH (phytanoyl-CoA 2-hydroxylase, also known as PAHX), an Fe(II) and 2OG (2-oxoglutarate) oxygenase, catalyses hydroxylation of phytanoyl-CoA. Mutations of PhyH ablate its role in α-oxidation, resulting in PA accumulation and ARD (adult Refsum's disease). The structure and function of PhyH is discussed in terms of its clinical importance and unusual selectivity. Most point mutations of PhyH causing ARD cluster in two distinct groups around the Fe(II)- and 2OG-binding sites. Therapaeutic possibilities for the treatment of Refsum's disease involving PhyH are discussed.

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