scholarly journals Crystal Structure of the Ancient, Fe−S Scaffold IscA Reveals a Novel Protein Fold†

Biochemistry ◽  
2004 ◽  
Vol 43 (1) ◽  
pp. 133-139 ◽  
Author(s):  
Patrick W. Bilder ◽  
Huangen Ding ◽  
Marcia E. Newcomer
Keyword(s):  
Crystal Structure ◽  
Protein Fold ◽  
Novel Protein

scholarly journals Crystallographic Studies of Human MitoNEET

2007 ◽  
Vol 282 (46) ◽  
pp. 33242-33246 ◽  
Author(s):  
Xiaowei Hou ◽  
Rujuan Liu ◽  
Stuart Ross ◽  
Eric J. Smart ◽  
Haining Zhu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mitochondrial Membrane ◽  
Hydrophobic Interactions ◽  
Water Molecules ◽  
Outer Mitochondrial Membrane ◽  
Protein Fold ◽  
Close Proximity ◽  
Diabetes Drug ◽  
Mitochondrial Membrane Protein ◽  
Novel Protein

MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone. The crystal structure of the cytoplasmic mitoNEET (residues 33–108) is determined in this study. The structure presents a novel protein fold and contains a [2Fe-2S] cluster-binding domain. The [2Fe-2S] cluster is coordinated to the protein by Cys-72, Cys-74, Cys-83, and His-87 residues. This coordination is also novel compared with the traditional [2Fe-2S] cluster coordinated by four cysteines or two cysteines and two histidines. The cytoplasmic mitoNEET forms homodimers in solution and in crystal. The dimerization is mainly mediated by hydrophobic interactions as well as hydrogen bonds coordinated by two water molecules binding at the interface. His-87 residue, which plays an important role in the coordination of the [2Fe-2S] cluster, is exposed to the solvent on the dimer surface. It is proposed that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster.

Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold

2020 ◽  
Vol 521 (3) ◽  
pp. 799-805
Author(s):  
Xiaofang Chen ◽  
Shan Liu ◽  
Sha Jiang ◽  
Xuecheng Zhang ◽  
Nannan Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Legionella Pneumophila ◽  
Protein Fold ◽  
Novel Protein

The crystal structure of NGO0477 from Neisseria gonorrhoeae reveals a novel protein fold incorporating a helix-turn-helix motif

2010 ◽  
Vol 78 (7) ◽  
pp. 1798-1802 ◽  
Author(s):  
Jingshan Ren ◽  
Sarah Sainsbury ◽  
Joanne E. Nettleship ◽  
Nigel J. Saunders ◽  
Raymond J. Owens
Keyword(s):  
Crystal Structure ◽  
Neisseria Gonorrhoeae ◽  
Protein Fold ◽  
Novel Protein

Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure

2001 ◽  
Vol 79 (8) ◽  
pp. 692-704 ◽  
Author(s):  
Focco van den Akker
Keyword(s):  
Crystal Structure ◽  
Atrial Natriuretic Factor ◽  
Binding Protein ◽  
Chloride Ion ◽  
Binding Domain ◽  
Protein Fold ◽  
Hormone Binding ◽  
Periplasmic Binding Protein ◽  
Natriuretic Factor ◽  
Hormone Binding Domain

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

scholarly journals X-ray crystal structure of MTH938 fromMethanobacterium thermoautotrophicumat 2.2 Å resolution reveals a novel tertiary protein fold

2001 ◽  
Vol 45 (4) ◽  
pp. 486-488 ◽  
Author(s):  
Kalyan Das ◽  
Rong Xiao ◽  
Elisabet Wahlberg ◽  
Fred Hsu ◽  
Cheryl H. Arrowsmith ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Fold ◽  
X Ray

scholarly journals The terminal phycobilisome emitter, LCM: A light-harvesting pigment with a phytochrome chromophore

2015 ◽  
Vol 112 (52) ◽  
pp. 15880-15885 ◽  
Author(s):  
Kun Tang ◽  
Wen-Long Ding ◽  
Astrid Höppner ◽  
Cheng Zhao ◽  
Lun Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transient Absorption ◽  
Light Harvesting ◽  
Reaction Centers ◽  
Protein Fold ◽  
Light Harvesting Complexes ◽  
Exciton Coupling ◽  
Femtosecond Transient Absorption ◽  
Orange Carotenoid Protein ◽  
Sensory Photoreceptors

Photosynthesis relies on energy transfer from light-harvesting complexes to reaction centers. Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, attach to the membrane via the multidomain core-membrane linker, LCM. The chromophore domain of LCM forms a bottleneck for funneling the harvested energy either productively to reaction centers or, in case of light overload, to quenchers like orange carotenoid protein (OCP) that prevent photodamage. The crystal structure of the solubly modified chromophore domain from Nostoc sp. PCC7120 was resolved at 2.2 Å. Although its protein fold is similar to the protein folds of phycobiliproteins, the phycocyanobilin (PCB) chromophore adopts ZZZssa geometry, which is unknown among phycobiliproteins but characteristic for sensory photoreceptors (phytochromes and cyanobacteriochromes). However, chromophore photoisomerization is inhibited in LCM by tight packing. The ZZZssa geometry of the chromophore and π-π stacking with a neighboring Trp account for the functionally relevant extreme spectral red shift of LCM. Exciton coupling is excluded by the large distance between two PCBs in a homodimer and by preservation of the spectral features in monomers. The structure also indicates a distinct flexibility that could be involved in quenching. The conclusions from the crystal structure are supported by femtosecond transient absorption spectra in solution.

scholarly journals Crystal Structure of TruD, a Novel Pseudouridine Synthase with a New Protein Fold

2004 ◽  
Vol 279 (18) ◽  
pp. 18107-18110 ◽  
Author(s):  
Yusuf Kaya ◽  
Mark Del Campo ◽  
James Ofengand ◽  
Arun Malhotra
Keyword(s):  
Crystal Structure ◽  
Protein Fold ◽  
Pseudouridine Synthase ◽  
New Protein

scholarly journals Crystal Structure of Chorismate Synthase: A Novel FMN-binding Protein Fold and Functional Insights

2004 ◽  
Vol 336 (4) ◽  
pp. 903-915 ◽  
Author(s):  
Hyung Jun Ahn ◽  
Hye-Jin Yoon ◽  
Byung Il Lee ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
Binding Protein ◽  
Protein Fold ◽  
Chorismate Synthase
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