1k39: Difference between revisions
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==The structure of yeast delta3-delta2-enoyl-COA isomerase complexed with octanoyl-COA== | ==The structure of yeast delta3-delta2-enoyl-COA isomerase complexed with octanoyl-COA== | ||
<StructureSection load='1k39' size='340' side='right' caption='[[1k39]], [[Resolution|resolution]] 3.29Å' scene=''> | <StructureSection load='1k39' size='340' side='right' caption='[[1k39]], [[Resolution|resolution]] 3.29Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] </span></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=1k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k39 OCA], [http://pdbe.org/1k39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k39 RCSB], [http://www.ebi.ac.uk/pdbsum/1k39 PDBsum]</span></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=1k39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k39 OCA], [http://pdbe.org/1k39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k39 RCSB], [http://www.ebi.ac.uk/pdbsum/1k39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k39 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=1k39 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 10:34, 11 October 2017
The structure of yeast delta3-delta2-enoyl-COA isomerase complexed with octanoyl-COAThe structure of yeast delta3-delta2-enoyl-COA isomerase complexed with octanoyl-COA
Structural highlights
Function[ECI1_YEAST] Essential for the beta oxidation of unsaturated fatty acids.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3--activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the beta4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8-15 form two turns of helix and pack against the H4-beta5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation. Crystal structure of an activated response regulator bound to its target.,Lee SY, Cho HS, Pelton JG, Yan D, Henderson RK, King DS, Huang L, Kustu S, Berry EA, Wemmer DE Nat Struct Biol. 2001 Jan;8(1):52-6. PMID:11135671[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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