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4y7v

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Revision as of 08:02, 3 May 2023

Structural analysis of MurU

Structural highlights

4y7v is a 1 chain structure with sequence from Pseudomonas putida BIRD-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MURU_PSEPK Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P (PubMed:23831760, PubMed:25767118). Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc (PubMed:23831760). Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc (PubMed:23831760). Is not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates (PubMed:23831760). Cannot accept other nucleotide triphosphates (ATP, CTP, TTP, or GTP) than UTP (PubMed:25767118).^[1] ^[2]

Publication Abstract from PubMed

The N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylyltransferase MurU catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall. MurU is part of a recently identified cell wall recycling pathway in Gram-negative bacteria that bypasses the general de-novo biosynthesis of UDP-MurNAc and contributes to high intrinsic resistance to the antibiotic fosfomycin, which targets UDP-MurNAc de novo biosynthesis. To provide insights into substrate binding and specificity, we solved crystal structures of MurU of Pseudomonas putida in native and ligand-bound states at high resolution. With the help of these structures, critical enzyme- substrate interactions were identified that enable tight binding of MurNAc-alpha1P to the active site of MurU. The MurU structures define a "minimal domain" required for general nucleotidyltransferase activity. They furthermore provide a structural basis for the chemical design of inhibitors of MurU, which could serve as novel drugs in combination therapy against multi-resistant Gram-negative pathogens.

Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylytransferase MurU, a minimal sugar-nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens.,Renner-Schneck M, Hinderberger I, Gisin J, Exner T, Mayer C, Stehle T J Biol Chem. 2015 Mar 12. pii: jbc.M114.620989. PMID:25767118^[3]

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

References

↑ Gisin J, Schneider A, Nägele B, Borisova M, Mayer C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat Chem Biol. 2013 Aug;9(8):491-3. PMID:23831760 doi:10.1038/nchembio.1289
↑ Renner-Schneck M, Hinderberger I, Gisin J, Exner T, Mayer C, Stehle T. Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylytransferase MurU, a minimal sugar-nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J Biol Chem. 2015 Mar 12. pii: jbc.M114.620989. PMID:25767118 doi:http://dx.doi.org/10.1074/jbc.M114.620989
↑ Renner-Schneck M, Hinderberger I, Gisin J, Exner T, Mayer C, Stehle T. Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1P) uridylytransferase MurU, a minimal sugar-nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J Biol Chem. 2015 Mar 12. pii: jbc.M114.620989. PMID:25767118 doi:http://dx.doi.org/10.1074/jbc.M114.620989

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4y7v"

Categories: Large Structures | Pseudomonas putida BIRD-1 | Renner-Schneck MG | Stehle T

@@ Line 3: / Line 3: @@
 <StructureSection load='4y7v' size='340' side='right'caption='[[4y7v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4y7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psepb Psepb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y7V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4y7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_BIRD-1 Pseudomonas putida BIRD-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7V FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2PN:IMIDODIPHOSPHORIC+ACID'>2PN</scene>, <scene name='pdbligand=491:2-(ACETYLAMINO)-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>491</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2PN:IMIDODIPHOSPHORIC+ACID'>2PN</scene>, <scene name='pdbligand=491:2-(ACETYLAMINO)-3-O-[(1R)-1-CARBOXYETHYL]-2-DEOXY-1-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>491</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPUBIRD1_0444 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=931281 PSEPB])</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=4y7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7v OCA], [https://pdbe.org/4y7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7v RCSB], [https://www.ebi.ac.uk/pdbsum/4y7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7v ProSAT]</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=4y7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7v OCA], [http://pdbe.org/4y7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y7v RCSB], [http://www.ebi.ac.uk/pdbsum/4y7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7v ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MURU_PSEPK MURU_PSEPK] Catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P (PubMed:23831760, PubMed:25767118). Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP-MurNAc (PubMed:23831760). Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc (PubMed:23831760). Is not able to use GlcNAc-alpha-1P and GalNAc-alpha-1P as substrates (PubMed:23831760). Cannot accept other nucleotide triphosphates (ATP, CTP, TTP, or GTP) than UTP (PubMed:25767118).<ref>PMID:23831760</ref> <ref>PMID:25767118</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Psepb]]
+[[Category: Pseudomonas putida BIRD-1]]
-[[Category: Renner-Schneck, M G]]
+[[Category: Renner-Schneck MG]]
-[[Category: Stehle, T]]
+[[Category: Stehle T]]
-[[Category: Murnac-1p]]
-[[Category: Nucleotidyltransferase family protein]]
-[[Category: Rossmann fold]]
-[[Category: Transferase]]
-[[Category: Uridyltransferase]]

4y7v

From Proteopedia

Revision as of 08:02, 3 May 2023

Structural analysis of MurU

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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