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| - | ==CRYSTAL STRUCTURE OF PBP4A FROM BACILLUS SUBTILIS== | + | |
| - | <StructureSection load='1w5d' size='340' side='right' caption='[[1w5d]], [[Resolution|resolution]] 2.10Å' scene=''> | + | ==Crystal structure of PBP4a from Bacillus subtilis== |
| | + | <StructureSection load='1w5d' size='340' side='right'caption='[[1w5d]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W5D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W5D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1w5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5d OCA], [http://pdbe.org/1w5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w5d RCSB], [http://www.ebi.ac.uk/pdbsum/1w5d PDBsum]</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=1w5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5d OCA], [https://pdbe.org/1w5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w5d RCSB], [https://www.ebi.ac.uk/pdbsum/1w5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w5d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DACC_BACSU DACC_BACSU]] Catalyzes DD-carboxypeptidase and transpeptidation reactions.<ref>PMID:11160090</ref> | + | [https://www.uniprot.org/uniprot/DACC_BACSU DACC_BACSU] Catalyzes DD-carboxypeptidase and transpeptidation reactions.<ref>PMID:11160090</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/1w5d_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/1w5d_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Penicillin-binding protein|Penicillin-binding protein]] | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus subtilis]] | | [[Category: Bacillus subtilis]] |
| - | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Charlier, P]] | + | [[Category: Charlier P]] |
| - | [[Category: Duez, C]] | + | [[Category: Duez C]] |
| - | [[Category: Frere, J M]] | + | [[Category: Frere JM]] |
| - | [[Category: Herman, R]] | + | [[Category: Herman R]] |
| - | [[Category: Petrella, S]] | + | [[Category: Petrella S]] |
| - | [[Category: Sauvage, E]] | + | [[Category: Sauvage E]] |
| - | [[Category: Bacillus subtili]]
| + | |
| - | [[Category: Beta-lactam]]
| + | |
| - | [[Category: D-ala-d-ala-carboxypeptidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Penicillin-binding protein]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| - | [[Category: Peptidoglycan synthesis]]
| + | |
| Structural highlights
Function
DACC_BACSU Catalyzes DD-carboxypeptidase and transpeptidation reactions.[1]
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 PubMed
The genome of Bacillus subtilis encodes 16 penicillin-binding proteins (PBPs) involved in the synthesis and/or remodelling of the peptidoglycan during the complex life cycle of this sporulating Gram-positive rod-shaped bacterium. PBP4a (encoded by the dacC gene) is a low-molecular mass PBP clearly exhibiting in vitro DD-carboxypeptidase activity. We have solved the crystal structure of this protein alone and in complex with a peptide (D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine) that mimics the C-terminal end of the Bacillus peptidoglycan stem peptide. PBP4a is composed of three domains: the penicillin-binding domain with a fold similar to the class A beta-lactamase structure and two domains inserted between the conserved motifs 1 and 2 characteristic of the penicillin-recognizing enzymes. The soaking of PBP4a in a solution of D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine resulted in an adduct between PBP4a and a D-alpha-aminopimelyl-epsilon-D-alanine dipeptide and an unbound D-alanine, i.e. the products of acylation of PBP4a by D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine with the release of a D-alanine. The adduct also reveals a binding pocket specific to the diaminopimelic acid, the third residue of the peptidoglycan stem pentapeptide of B. subtilis. This pocket is specific for this class of PBPs.
Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide.,Sauvage E, Duez C, Herman R, Kerff F, Petrella S, Anderson JW, Adediran SA, Pratt RF, Frere JM, Charlier P J Mol Biol. 2007 Aug 10;371(2):528-39. Epub 2007 Jun 2. PMID:17582436[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Duez C, Vanhove M, Gallet X, Bouillenne F, Docquier J, Brans A, Frere J. Purification and characterization of PBP4a, a new low-molecular-weight penicillin-binding protein from Bacillus subtilis. J Bacteriol. 2001 Mar;183(5):1595-9. PMID:11160090 doi:10.1128/JB.183.5.1595-1599.2001
- ↑ Sauvage E, Duez C, Herman R, Kerff F, Petrella S, Anderson JW, Adediran SA, Pratt RF, Frere JM, Charlier P. Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide. J Mol Biol. 2007 Aug 10;371(2):528-39. Epub 2007 Jun 2. PMID:17582436 doi:10.1016/j.jmb.2007.05.071
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