scholarly journals 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

2014 ◽  
Vol 70 (4) ◽  
pp. 418-423 ◽  
Author(s):  
Chingakham R. Singh ◽  
Scott Lovell ◽  
Nurjahan Mehzabeen ◽  
Wasimul Q. Chowdhury ◽  
Eric S. Geanes ◽  
...  
Keyword(s):  
Pdz Domain ◽  
Structure And Function ◽  
26S Proteasome ◽  
Atpase Subunit ◽  
Aaa Atpase ◽  
Ubiquitinated Proteins ◽  
C Terminus ◽  
And Function ◽  
Resolution Structure

The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.

Structure and Function Relationship of Murine Insulin-like Peptide 5 (INSL5): Free C-Terminus Is Essential for RXFP4 Receptor Binding and Activation

Biochemistry ◽  
2011 ◽  
Vol 50 (39) ◽  
pp. 8352-8361 ◽  
Author(s):  
Alessia Belgi ◽  
Mohammed A. Hossain ◽  
Fazel Shabanpoor ◽  
Linda Chan ◽  
Suode Zhang ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Structure And Function ◽  
C Terminus ◽  
Function Relationship ◽  
Structure And Function Relationship ◽  
And Function ◽  
Relationship Of

Role of the C-Terminus of the High-Conductance Calcium-Activated Potassium Channel in Channel Structure and Function

Biochemistry ◽  
2005 ◽  
Vol 44 (30) ◽  
pp. 10135-10144 ◽  
Author(s):  
William A. Schmalhofer ◽  
Manuel Sanchez ◽  
Ge Dai ◽  
Ashvin Dewan ◽  
Lorena Secades ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Structure And Function ◽  
Channel Structure ◽  
C Terminus ◽  
And Function ◽  
Calcium Activated Potassium Channel ◽  
High Conductance

Compartmentalized NRG signaling and PDZ domain‐containing proteins in synapse structure and function

2002 ◽  
Vol 20 (3-5) ◽  
pp. 173-185 ◽  
Author(s):  
Yang Z. Huang ◽  
Qiang Wang ◽  
Sandra Won ◽  
Zhen G. Luo ◽  
Wen C. Xiong ◽  
...  
Keyword(s):  
Pdz Domain ◽  
Structure And Function ◽  
And Function

scholarly journals Fundamental Characteristics of AAA+ Protein Family Structure and Function

Archaea ◽  
2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Justin M. Miller ◽  
Eric J. Enemark
Keyword(s):  
Atp Hydrolysis ◽  
Molecular Machines ◽  
Ring Structure ◽  
Structure And Function ◽  
Central Channel ◽  
Aaa Atpase ◽  
Cellular Events ◽  
Critical Components ◽  
And Function ◽  
Aaa Protein

Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities) are critical components of many molecular machines. AAA+ proteins are defined by conserved modules that precisely position the active site elements of two adjacent subunits to catalyze ATP hydrolysis. In many cases, AAA+ proteins form a ring structure that translocates a polymeric substrate through the central channel using specialized loops that project into the central channel. We discuss the major features of AAA+ protein structure and function with an emphasis on pivotal aspects elucidated with archaeal proteins.

A urea channel from Bacillus cereus reveals a novel hexameric structure

2012 ◽  
Vol 445 (2) ◽  
pp. 157-166 ◽  
Author(s):  
Gerard H. M. Huysmans ◽  
Nathan Chan ◽  
Jocelyn M. Baldwin ◽  
Vincent L. G. Postis ◽  
Svetomir B. Tzokov ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Structure And Function ◽  
Size Exclusion ◽  
Fluorescent Labelling ◽  
Transmembrane Helices ◽  
Cryo Electron Microscopy ◽  
C Terminus ◽  
Exclusion Chromatography ◽  
Urea Channel ◽  
And Function

Urea is exploited as a nitrogen source by bacteria, and its breakdown products, ammonia and bicarbonate, are employed to counteract stomach acidity in pathogens such as Helicobacter pylori. Uptake in the latter is mediated by UreI, a UAC (urea amide channel) family member. In the present paper, we describe the structure and function of UACBc, a homologue from Bacillus cereus. The purified channel was found to be permeable not only to urea, but also to other small amides. CD and IR spectroscopy revealed a structure comprising mainly α-helices, oriented approximately perpendicular to the membrane. Consistent with this finding, site-directed fluorescent labelling indicated the presence of seven TM (transmembrane) helices, with a cytoplasmic C-terminus. In detergent, UACBc exists largely as a hexamer, as demonstrated by both cross-linking and size-exclusion chromatography. A 9 Å (1 Å=0.1 nm) resolution projection map obtained by cryo-electron microscopy of two-dimensional crystals shows that the six protomers are arranged in a planar hexameric ring. Each exhibits six density features attributable to TM helices, surrounding a putative central channel, while an additional helix is peripherally located. Bioinformatic analyses allowed individual TM regions to be tentatively assigned to the density features, with the resultant model enabling identification of residues likely to contribute to channel function.

scholarly journals Assembly, structure, and function of the 26S proteasome

2010 ◽  
Vol 20 (7) ◽  
pp. 391-401 ◽  
Author(s):  
Lynn Bedford ◽  
Simon Paine ◽  
Paul W. Sheppard ◽  
R. John Mayer ◽  
Jeroen Roelofs
Keyword(s):  
Structure And Function ◽  
26S Proteasome ◽  
Assembly Structure ◽  
And Function

scholarly journals Structure and function of the AAA+ ATPase p97/Cdc48p

Gene ◽  
2016 ◽  
Vol 583 (1) ◽  
pp. 64-77 ◽  
Author(s):  
Di Xia ◽  
Wai Kwan Tang ◽  
Yihong Ye
Keyword(s):  
Structure And Function ◽  
Aaa Atpase ◽  
And Function

scholarly journals Structural Adaptation of Cold-Active RTX Lipase fromPseudomonassp. Strain AMS8 Revealed via Homology and Molecular Dynamics Simulation Approaches

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Mohd. Shukuri Mohamad Ali ◽  
Siti Farhanie Mohd Fuzi ◽  
Menega Ganasen ◽  
Raja Noor Zaliha Raja Abdul Rahman ◽  
Mahiran Basri ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Industrial Applications ◽  
Structure And Function ◽  
Molecular Engineering ◽  
Dynamics Simulation ◽  
Structural Adaptation ◽  
C Terminus ◽  
Different Temperatures ◽  
And Function ◽  
3D Molecular Structure

The psychrophilic enzyme is an interesting subject to study due to its special ability to adapt to extreme temperatures, unlike typical enzymes. Utilizing computer-aided software, the predicted structure and function of the enzyme lipase AMS8 (LipAMS8) (isolated from the psychrophilicPseudomonassp., obtained from the Antarctic soil) are studied. The enzyme shows significant sequence similarities with lipases fromPseudomonassp. MIS38 andSerratia marcescens. These similarities aid in the prediction of the 3D molecular structure of the enzyme. In this study, 12 ns MD simulation is performed at different temperatures for structural flexibility and stability analysis. The results show that the enzyme is most stable at 0°C and 5°C. In terms of stability and flexibility, the catalytic domain (N-terminus) maintained its stability more than the noncatalytic domain (C-terminus), but the non-catalytic domain showed higher flexibility than the catalytic domain. The analysis of the structure and function of LipAMS8 provides new insights into the structural adaptation of this protein at low temperatures. The information obtained could be a useful tool for low temperature industrial applications and molecular engineering purposes, in the near future.

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