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3zh4

From Proteopedia

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crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate

Structural highlights

3zh4 is a 1 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MURA1_STRPI Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine (By similarity). Target for the antibiotic fosfomycin.[HAMAP-Rule:MF_00111]^[1]

Publication Abstract from PubMed

Fosfomycin 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Engel H, Gutierrez-Fernandez J, Fluckiger C, Martinez-Ripoll M, Muhlemann K, Hermoso JA, Hilty M, Hathaway LJ. Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on murA1 gene. Antimicrob Agents Chemother. 2013 Apr 9. PMID:23571543 doi:10.1128/AAC.00223-13
↑ Engel H, Gutierrez-Fernandez J, Fluckiger C, Martinez-Ripoll M, Muhlemann K, Hermoso JA, Hilty M, Hathaway LJ. Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on murA1 gene. Antimicrob Agents Chemother. 2013 Apr 9. PMID:23571543 doi:10.1128/AAC.00223-13

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zh4"

Categories: Large Structures | Streptococcus pneumoniae | Gutierrez-Fernandez J | Hermoso JA

@@ Line 3: / Line 3: @@
 <StructureSection load='3zh4' size='340' side='right'caption='[[3zh4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zh4]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3ZH4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zh4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3ZH4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.8&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3zh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zh4 OCA], [https://pdbe.org/3zh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zh4 RCSB], [https://www.ebi.ac.uk/pdbsum/3zh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zh4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/B1IBM3_STRPI B1IBM3_STRPI]] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.[HAMAP-Rule:MF_00111][SAAS:SAAS00085359]
+[https://www.uniprot.org/uniprot/MURA1_STRPI MURA1_STRPI] Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine (By similarity). Target for the antibiotic fosfomycin.[HAMAP-Rule:MF_00111]<ref>PMID:23571543</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: UDP-N-acetylglucosamine 1-carboxyvinyltransferase]]
+[[Category: Streptococcus pneumoniae]]
-[[Category: Gutierrez-Fernandez, J]]
+[[Category: Gutierrez-Fernandez J]]
-[[Category: Hermoso, J A]]
+[[Category: Hermoso JA]]
-[[Category: Mura]]
-[[Category: Transferase]]

3zh4

From Proteopedia

Current revision

crystal structure of S. pneumoniae Hungary 19A MurA1 in complex with citrate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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