5ipw
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==oligopeptide-binding protein OppA== | |
+ | <StructureSection load='5ipw' size='340' side='right' caption='[[5ipw]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5ipw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IPW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IPW FirstGlance]. <br> | ||
+ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ipw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ipw OCA], [http://pdbe.org/5ipw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ipw RCSB], [http://www.ebi.ac.uk/pdbsum/5ipw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ipw ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Oligopeptide-binding proteins (Opps) are part of the ATP-binding cassette system, playing a crucial role in nutrient uptake and sensing the external environment in bacteria, including hyperthermophiles. Opps serve as a binding platform for diverse peptides; however, how these peptides are recognized by Opps is still largely unknown and few crystal structures of Opps from hyperthermophiles have been determined. To facilitate such an understanding, the crystal structure of a putative Opp, OppA from Thermotoga maritima (TmOppA), was solved at 2.6-A resolution in the open conformation. TmOppA is composed of three domains. The N-terminal domain consists of twelve strands, nine helices, and four 310 helices, and the C-terminal domain consists of five strands, ten helices, and one 310 helix. These two domains are connected by the linker domain, which consists of two strands, three helices, and three 310 helices. Based on structural comparisons of TmOppA with other OppAs and binding studies, we suggest that TmOppA might be a periplasmic Opp. The most distinct feature of TmOppA is the insertion of two helices, which are lacking in other OppAs. A cavity volume between the N-terminal and C-terminal domains is suggested to be responsible for binding peptides of various lengths. | ||
- | + | Crystal structure of a putative oligopeptide-binding periplasmic protein from a hyperthermophile.,Yoon HJ, Kim HJ, Mikami B, Yu YG, Lee HH Extremophiles. 2016 Sep;20(5):723-31. doi: 10.1007/s00792-016-0861-7. Epub 2016, Jul 5. PMID:27377296<ref>PMID:27377296</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Lee, H | + | <div class="pdbe-citations 5ipw" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Kim, H J]] | ||
+ | [[Category: Lee, H H]] | ||
+ | [[Category: Yoon, H J]] | ||
+ | [[Category: Oligopeptide-binding protein]] | ||
+ | [[Category: Peptide binding protein]] |
Revision as of 21:04, 15 March 2017
oligopeptide-binding protein OppA
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