4bub: Difference between revisions
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<StructureSection load='4bub' size='340' side='right'caption='[[4bub]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='4bub' size='340' side='right'caption='[[4bub]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bub]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4bub]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4bub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bub OCA], [https://pdbe.org/4bub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bub RCSB], [https://www.ebi.ac.uk/pdbsum/4bub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bub ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MURE_THEMA MURE_THEMA] Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently.<ref>PMID:16595662</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Contreras-Martel | [[Category: Thermotoga maritima]] | ||
[[Category: Dessen | [[Category: Contreras-Martel C]] | ||
[[Category: Favini-Stabile | [[Category: Dessen A]] | ||
[[Category: Thielens | [[Category: Favini-Stabile S]] | ||
[[Category: Thielens N]] | |||
Latest revision as of 11:17, 9 October 2024
CRYSTAL STRUCTURE OF MURE LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADPCRYSTAL STRUCTURE OF MURE LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP
Structural highlights
FunctionMURE_THEMA Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently.[1] Publication Abstract from PubMedPeptidoglycan is a major determinant of cell shape in bacteria, and its biosynthesis involves the concerted action of cytoplasmic, membrane-associated and periplasmic enzymes. Within the cytoplasm, Mur enzymes catalyse the first steps leading to peptidoglycan precursor biosynthesis, and have been suggested as being part of a multicomponent complex that could also involve the transglycosylase MurG and the cytoskeletal protein MreB. In order to initialize the characterization of a potential Mur interaction network, we purified MurD, MurE, MurF, MurG and MreB from Thermotoga maritima and characterized their interactions using membrane blotting and surface plasmon resonance. MurD, MurE and MurF all recognize MurG and MreB, but not each other, while the two latter proteins interact. In addition, we solved the crystal structures of MurD, MurE and MurF, which indicate that their C-termini display high conformational flexibilities. The differences in Mur conformations could be important parameters for the stability of an intracytoplasmic murein biosynthesis complex. MreB and MurG as scaffolds for the cytoplasmic steps of peptidoglycan biosynthesis.,Favini-Stabile S, Contreras-Martel C, Thielens N, Dessen A Environ Microbiol. 2013 Jun 3. doi: 10.1111/1462-2920.12171. PMID:23826965[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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