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| | <StructureSection load='3opb' size='340' side='right'caption='[[3opb]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3opb' size='340' side='right'caption='[[3opb]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3opb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OPB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3opb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OPB FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SHE4, YOR035C, OR26.26 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3opb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opb OCA], [https://pdbe.org/3opb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3opb RCSB], [https://www.ebi.ac.uk/pdbsum/3opb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3opb ProSAT]</span></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=3opb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3opb OCA], [https://pdbe.org/3opb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3opb RCSB], [https://www.ebi.ac.uk/pdbsum/3opb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3opb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SHE4_YEAST SHE4_YEAST]] Required for mother cell-specific ho expression. Might be required for the transport of factors (such as ASH1) that promote HO repression from the mother cell into its bud.
| + | [https://www.uniprot.org/uniprot/SHE4_YEAST SHE4_YEAST] Required for mother cell-specific ho expression. Might be required for the transport of factors (such as ASH1) that promote HO repression from the mother cell into its bud. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | UNC-45/CRO1/She4p (UCS) proteins have variously been proposed to affect the folding, stability, and ATPase activity of myosins. They are the only proteins known to interact directly with the motor domain. To gain more insight into UCS function, we determined the atomic structure of the yeast UCS protein, She4p, at 2.9 A resolution. We found that 16 helical repeats are organized into an L-shaped superhelix with an amphipathic N-terminal helix dangling off the short arm of the L-shaped molecule. In the crystal, She4p forms a 193-A-long, zigzag-shaped dimer through three distinct and evolutionary conserved interfaces. We have identified She4p's C-terminal region as a ligand for a 27-residue-long epitope on the myosin motor domain. Remarkably, this region consists of two adjacent, but distinct, binding epitopes localized at the nucleotide-responsive cleft between the nucleotide- and actin-filament-binding sites. One epitope is situated inside the cleft, the other outside the cleft. After ATP hydrolysis and Pi ejection, the cleft narrows at its base from 20 to 12 A thereby occluding the inside the cleft epitope, while leaving the adjacent, outside the cleft binding epitope accessible to UCS binding. Hence, one cycle of higher and lower binding affinity would accompany one ATP hydrolysis cycle and a single step in the walk on an actin filament rope. We propose that a UCS dimer links two myosins at their motor domains and thereby functions as one of the determinants for step size of myosin on actin filaments.
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| - | UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.,Shi H, Blobel G Proc Natl Acad Sci U S A. 2010 Nov 29. PMID:21115842<ref>PMID:21115842</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3opb" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blobel, G]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Shi, H]] | + | [[Category: Blobel G]] |
| - | [[Category: Heat and arm fold]] | + | [[Category: Shi H]] |
| - | [[Category: Myosin binding protein]]
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| - | [[Category: Myosin folding and function]]
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| - | [[Category: Protein binding]]
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