1oi6: Difference between revisions
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New page: left|200px<br /> <applet load="1oi6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oi6, resolution 1.40Å" /> '''STRUCTURE DETERMINA... |
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== | ==Structure determination of the TMP-complex of EvaD== | ||
Vancomycin, the last line of defense antibiotic, depends upon the | <StructureSection load='1oi6' size='340' side='right'caption='[[1oi6]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1oi6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OI6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></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=1oi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oi6 OCA], [https://pdbe.org/1oi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oi6 RCSB], [https://www.ebi.ac.uk/pdbsum/1oi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oi6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O52806_AMYOR O52806_AMYOR] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oi/1oi6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</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/main_output.php?pdb_ID=1oi6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vancomycin, the last line of defense antibiotic, depends upon the attachment of the carbohydrate vancosamine to an aglycone skeleton for antibacterial activity. Vancomycin is a naturally occurring secondary metabolite that can be produced by bacterial fermentation. To combat emerging resistance, it has been proposed to genetically engineer bacteria to produce analogues of vancomycin. This requires a detailed understanding of the biochemical steps in the synthesis of vancomycin. Here we report the 1.4 A structure and biochemical characterization of EvaD, an RmlC-like protein that is required for the C-5' epimerization during synthesis of dTDP-epivancosamine. EvaD, although clearly belonging to the RmlC class of enzymes, displays very low activity in the archetypal RmlC reaction (double epimerization of dTDP-6-deoxy-4-keto-D-glucose at C-3' and C-5'). The high resolution structure of EvaD compared with the structures of authentic RmlC enzymes indicates that a subtle change in the enzyme active site repositions a key catalytic Tyr residue. A mutant designed to re-establish the normal position of the Tyr increases the RmlC-like activity of EvaD. | |||
The position of a key tyrosine in dTDP-4-Keto-6-deoxy-D-glucose-5-epimerase (EvaD) alters the substrate profile for this RmlC-like enzyme.,Merkel AB, Major LL, Errey JC, Burkart MD, Field RA, Walsh CT, Naismith JH J Biol Chem. 2004 Jul 30;279(31):32684-91. Epub 2004 May 24. PMID:15159413<ref>PMID:15159413</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1oi6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Amycolatopsis orientalis]] | [[Category: Amycolatopsis orientalis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Merkel | [[Category: Merkel AB]] | ||
[[Category: Naismith | [[Category: Naismith JH]] | ||
Latest revision as of 12:41, 13 December 2023
Structure determination of the TMP-complex of EvaD
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