8f5d: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8f5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_18323 Bordetella pertussis 18323]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F5D FirstGlance]. <br>
<table><tr><td colspan='2'>[[8f5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis_18323 Bordetella pertussis 18323]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F5D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.56&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8f5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f5d OCA], [https://pdbe.org/8f5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f5d RCSB], [https://www.ebi.ac.uk/pdbsum/8f5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f5d ProSAT]</span></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=8f5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f5d OCA], [https://pdbe.org/8f5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f5d RCSB], [https://www.ebi.ac.uk/pdbsum/8f5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f5d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A0T7CQ89_BORP1 A0A0T7CQ89_BORP1] Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.[HAMAP-Rule:MF_00208]  Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[HAMAP-Rule:MF_02019][RuleBase:RU004136]
[https://www.uniprot.org/uniprot/A0A0T7CQ89_BORP1 A0A0T7CQ89_BORP1] Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.[HAMAP-Rule:MF_00208]  Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[HAMAP-Rule:MF_02019][RuleBase:RU004136]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan (PG) is a central component of the bacterial cell wall, and the disruption of its biosynthetic pathway has been a successful antibacterial strategy for decades. PG biosynthesis is initiated in the cytoplasm through sequential reactions catalyzed by Mur enzymes that have been suggested to associate into a multimembered complex. This idea is supported by the observation that in many eubacteria, mur genes are present in a single operon within the well conserved dcw cluster, and in some cases, pairs of mur genes are fused to encode a single, chimeric polypeptide. We performed a vast genomic analysis using &gt;140 bacterial genomes and mapped Mur chimeras in numerous phyla, with Proteobacteria carrying the highest number. MurE-MurF, the most prevalent chimera, exists in forms that are either directly associated or separated by a linker. The crystal structure of the MurE-MurF chimera from Bordetella pertussis reveals a head-to-tail, elongated architecture supported by an interconnecting hydrophobic patch that stabilizes the positions of the two proteins. Fluorescence polarization assays reveal that MurE-MurF interacts with other Mur ligases via its central domains with K(D)s in the high nanomolar range, backing the existence of a Mur complex in the cytoplasm. These data support the idea of stronger evolutionary constraints on gene order when encoded proteins are intended for association, establish a link between Mur ligase interaction, complex assembly and genome evolution, and shed light on regulatory mechanisms of protein expression and stability in pathways of critical importance for bacterial survival.
Architecture and genomic arrangement of the MurE-MurF bacterial cell wall biosynthesis complex.,Shirakawa KT, Sala FA, Miyachiro MM, Job V, Trindade DM, Dessen A Proc Natl Acad Sci U S A. 2023 May 23;120(21):e2219540120. doi: , 10.1073/pnas.2219540120. Epub 2023 May 15. PMID:37186837<ref>PMID:37186837</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8f5d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 10:27, 3 April 2024

Architecture of the MurE-MurF ligase bacterial cell wall biosynthesis complexArchitecture of the MurE-MurF ligase bacterial cell wall biosynthesis complex

Structural highlights

8f5d is a 1 chain structure with sequence from Bordetella pertussis 18323. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.56Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0T7CQ89_BORP1 Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.[HAMAP-Rule:MF_00208] Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[HAMAP-Rule:MF_02019][RuleBase:RU004136]

8f5d, resolution 2.56Å

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