8f5d
From Proteopedia
(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]] 2.56Å</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 >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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 8f5d" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Architecture of the MurE-MurF ligase bacterial cell wall biosynthesis complex
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