2hg4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.== | ==Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.== | ||
<StructureSection load='2hg4' size='340' side='right' caption='[[2hg4]], [[Resolution|resolution]] 2.73Å' scene=''> | <StructureSection load='2hg4' size='340' side='right'caption='[[2hg4]], [[Resolution|resolution]] 2.73Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hg4]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2hg4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_erythreus"_(sic)_waksman_1923 "actinomyces erythreus" (sic) waksman 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HG4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eryA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eryA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1836 "Actinomyces erythreus" (sic) Waksman 1923])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/6-deoxyerythronolide-B_synthase 6-deoxyerythronolide-B synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.94 2.3.1.94] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hg4 OCA], [https://pdbe.org/2hg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hg4 RCSB], [https://www.ebi.ac.uk/pdbsum/2hg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hg4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
*[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]] | *[[6-deoxyerythronolide B synthase (DEBS)|6-deoxyerythronolide B synthase (DEBS)]] | ||
*[[6-deoxyerythronolide B synthase 3D structures|6-deoxyerythronolide B synthase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 37: | Line 38: | ||
</StructureSection> | </StructureSection> | ||
[[Category: 6-deoxyerythronolide-B synthase]] | [[Category: 6-deoxyerythronolide-B synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: Cane, D E]] | [[Category: Cane, D E]] | ||
[[Category: Khosla, C]] | [[Category: Khosla, C]] | ||
Revision as of 10:39, 17 March 2021
Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.Structure of the ketosynthase-acyltransferase didomain of module 5 from DEBS.
Structural highlights
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 x-ray crystal structure of a 194-kDa fragment from module 5 of the 6-deoxyerythronolide B synthase has been solved at 2.7 Angstrom resolution. Each subunit of the homodimeric protein contains a full-length ketosynthase (KS) and acyl transferase (AT) domain as well as three flanking "linkers." The linkers are structurally well defined and contribute extensively to intersubunit or interdomain interactions, frequently by means of multiple highly conserved residues. The crystal structure also reveals that the active site residue Cys-199 of the KS domain is separated from the active site residue Ser-642 of the AT domain by approximately 80 Angstrom. This distance is too large to be covered simply by alternative positioning of a statically anchored, fully extended phosphopantetheine arm of the acyl carrier protein domain from module 5. Thus, substantial domain reorganization appears necessary for the acyl carrier protein to interact successively with both the AT and the KS domains of this prototypical polyketide synthase module. The 2.7-Angstrom KS-AT structure is fully consistent with a recently reported lower resolution, 4.5-Angstrom model of fatty acid synthase structure, and emphasizes the close biochemical and structural similarity between polyketide synthase and fatty acid synthase enzymology. The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase.,Tang Y, Kim CY, Mathews II, Cane DE, Khosla C Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11124-9. Epub 2006 Jul 14. PMID:16844787[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||||||