3zh4: Difference between revisions
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==crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate== | ==crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate== | ||
<StructureSection load='3zh4' size='340' side='right' caption='[[3zh4]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3zh4' size='340' side='right' caption='[[3zh4]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zh4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3zh4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZH4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZH4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </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=3zh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zh4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zh4 RCSB], [http://www.ebi.ac.uk/pdbsum/3zh4 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=3zh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zh4 OCA], [http://pdbe.org/3zh4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zh4 RCSB], [http://www.ebi.ac.uk/pdbsum/3zh4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zh4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/B1IBM3_STRPI B1IBM3_STRPI]] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.[HAMAP-Rule:MF_00111][SAAS:SAAS00085359] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zh4" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]] | [[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]] | ||
[[Category: Gutierrez-Fernandez, J]] | [[Category: Gutierrez-Fernandez, J]] | ||
Revision as of 11:30, 11 August 2016
crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citratecrystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate
Structural highlights
Function[B1IBM3_STRPI] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.[HAMAP-Rule:MF_00111][SAAS:SAAS00085359] Publication Abstract from PubMedFosfomycin targets the first step of peptidoglycan biosynthesis in Streptococcus pneumoniae catalyzed by UDP-N-acetylglucosamine enolpyruvyltransferase (MurA1). We investigated whether heteroresistance to fosfomycin occurs in S. pneumoniae. We found that of 11 strains tested all but one (Hungary19A) displayed heteroresistance and that deletion of murA1 abolished heteroresistance. Hungary19A differs from the other strains by a single amino-acid substitution in MurA1 (Ala364Thr). To test whether this substitution is responsible for lack of heteroresistance, it was introduced into strain D39. The heteroresistant phenotype of strain D39 was not changed. Furthermore, no relevant structural differences between MurA1 of the heteroresistant strain D39 or the non-heteroresistant strain Hungary19A were found in their crystal structures. Our results reveal that heteroresistance to fosfomycin is the predominant phenotype in S. pneumoniae and that MurA1 is required for heteroresistance to fosfomycin but is not the only factor involved. The findings provide a caveat for any future use of fosfomycin in the treatment of pneumococcal infections. Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on murA1 gene.,Engel H, Gutierrez-Fernandez J, Fluckiger C, Martinez-Ripoll M, Muhlemann K, Hermoso JA, Hilty M, Hathaway LJ Antimicrob Agents Chemother. 2013 Apr 9. PMID:23571543[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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