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4qr7
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation== |
| - | + | <StructureSection load='4qr7' size='340' side='right' caption='[[4qr7]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4qr7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QR7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DWZ:(2S,3R,4S)-4-{[(3S,5S)-5-(DIMETHYLCARBAMOYL)PYRROLIDIN-3-YL]SULFANYL}-2-[(1S,2R)-1-FORMYL-2-HYDROXYPROPYL]-3-METHYL-3,4-DIHYDRO-2H-PYRROLE-5-CARBOXYLIC+ACID'>DWZ</scene>, <scene name='pdbligand=MLD:GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA'>MLD</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qra|4qra]], [[4qrb|4qrb]]</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=4qr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qr7 RCSB], [http://www.ebi.ac.uk/pdbsum/4qr7 PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/LDT2_MYCTU LDT2_MYCTU]] Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap(3) of the donor stem and the side chain of mDap(3) of the acceptor stem. Is specific for donor substrates containing a stem tetrapeptide since it cannot use pentapeptide stems.<ref>PMID:24041897</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Structural genomic]] | ||
[[Category: Gokulan, K]] | [[Category: Gokulan, K]] | ||
| - | [[Category: | + | [[Category: Varughese, K I]] |
| + | [[Category: Beta-lactamase]] | ||
| + | [[Category: Csgid]] | ||
| + | [[Category: D-d-transpeptidase]] | ||
| + | [[Category: Enzyme function initiative]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Imipenem]] | ||
| + | [[Category: L-d-transpeptidase]] | ||
| + | [[Category: Meropenem]] | ||
| + | [[Category: Peptidoglycan]] | ||
| + | [[Category: Single anomalous diffraction]] | ||
Revision as of 14:46, 29 July 2015
Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation
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