1w79: Difference between revisions
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<StructureSection load='1w79' size='340' side='right'caption='[[1w79]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1w79' size='340' side='right'caption='[[1w79]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w79]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1w79]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp._R39 Actinomadura sp. R39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W79 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]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w79 OCA], [https://pdbe.org/1w79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w79 RCSB], [https://www.ebi.ac.uk/pdbsum/1w79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w79 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=1w79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w79 OCA], [https://pdbe.org/1w79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w79 RCSB], [https://www.ebi.ac.uk/pdbsum/1w79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w79 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Actinomadura sp. R39]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Charlier P]] | |||
[[Category: Charlier | [[Category: Duez C]] | ||
[[Category: Duez | [[Category: Frere JM]] | ||
[[Category: Frere | [[Category: Herman R]] | ||
[[Category: Herman | [[Category: Petrella S]] | ||
[[Category: Petrella | [[Category: Sauvage E]] | ||
[[Category: Sauvage | |||
Latest revision as of 12:12, 9 May 2024
Crystal structure of the DD-transpeptidase-carboxypeptidase from Actinomadura R39Crystal structure of the DD-transpeptidase-carboxypeptidase from Actinomadura R39
Structural highlights
FunctionDAC_ACTSP Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedActinomadura sp. R39 produces an exocellular DD-peptidase/penicillin-binding protein (PBP) whose primary structure is similar to that of Escherichia coli PBP4. It is characterized by a high beta-lactam-binding activity (second order rate constant for the acylation of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1)). The crystal structure of the DD-peptidase from Actinomadura R39 was solved at a resolution of 1.8 angstroms by single anomalous dispersion at the cobalt resonance wavelength. The structure is composed of three domains: a penicillin-binding domain similar to the penicillin-binding domain of E. coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the penicillin-binding domain. In R39, the other two domains are inserted in the penicillin-binding domain, between the SXXK and SXN motifs, in a manner similar to "Matryoshka dolls." One of these domains is composed of a five-stranded beta-sheet with two helices on one side, and the other domain is a double three-stranded beta-sheet inserted in the previous domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme complex of R39 with nitrocefin reveals the absence of active site conformational change upon binding the beta-lactams. Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins.,Sauvage E, Herman R, Petrella S, Duez C, Bouillenne F, Frere JM, Charlier P J Biol Chem. 2005 Sep 2;280(35):31249-56. Epub 2005 Jun 29. PMID:15987687[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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