1u9p
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='1u9p' size='340' side='right'caption='[[1u9p]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1u9p' size='340' side='right'caption='[[1u9p]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1u9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1u9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U9P FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9p OCA], [https://pdbe.org/1u9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9p RCSB], [https://www.ebi.ac.uk/pdbsum/1u9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9p ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9p OCA], [https://pdbe.org/1u9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9p RCSB], [https://www.ebi.ac.uk/pdbsum/1u9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RARC_BPP22 RARC_BPP22] This protein acts as a transcriptional repressor of its own gene arc and of gene ant. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 16: | Line 19: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u9p ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u9p ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | We designed a single-chain variant of the Arc repressor homodimer in which the beta strands that contact operator DNA are connected by a hairpin turn and the alpha helices that form the tetrahelical scaffold of the dimer are attached by a short linker. The designed protein represents a noncyclic permutation of secondary structural elements in another single-chain Arc molecule (Arc-L1-Arc), in which the two subunits are fused by a single linker. The permuted protein binds operator DNA with nanomolar affinity, refolds on the sub-millisecond time scale, and is as stable as Arc-L1-Arc. The crystal structure of the permuted protein reveals an essentially wild-type fold, demonstrating that crucial folding information is not encoded in the wild-type order of secondary structure. Noncyclic rearrangement of secondary structure may allow grouping of critical active-site residues in other proteins and could be a useful tool for protein design and minimization. | ||
- | |||
- | Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure.,Tabtiang RK, Cezairliyan BO, Grant RA, Cochrane JC, Sauer RT Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2305-9. Epub 2005 Feb 2. PMID:15689399<ref>PMID:15689399</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1u9p" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Cezairliyan | + | [[Category: Cezairliyan BO]] |
- | [[Category: Cochrane | + | [[Category: Cochrane JC]] |
- | [[Category: Grant | + | [[Category: Grant RA]] |
- | [[Category: Sauer | + | [[Category: Sauer RT]] |
- | [[Category: Tabtiang | + | [[Category: Tabtiang RK]] |
- | + | ||
- | + | ||
- | + |
Current revision
Permuted single-chain Arc
|