2j9p: Difference between revisions
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|PDB= 2j9p |SIZE=350|CAPTION= <scene name='initialview01'>2j9p</scene>, resolution 2.80Å | |PDB= 2j9p |SIZE=350|CAPTION= <scene name='initialview01'>2j9p</scene>, resolution 2.80Å | ||
|SITE= <scene name='pdbsite=AC1:Dal+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Dal+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=REZ:(2R)-2-AMINO-7-{[(1R)-1-CARBOXYETHYL]AMINO}-7-OXOHEPTANOIC ACID'>REZ</scene> | |LIGAND= <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=REZ:(2R)-2-AMINO-7-{[(1R)-1-CARBOXYETHYL]AMINO}-7-OXOHEPTANOIC+ACID'>REZ</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9p OCA], [http://www.ebi.ac.uk/pdbsum/2j9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j9p RCSB]</span> | |||
}} | }} | ||
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[[Category: Kerff, F.]] | [[Category: Kerff, F.]] | ||
[[Category: Sauvage, E.]] | [[Category: Sauvage, E.]] | ||
[[Category: bacillus subtili]] | [[Category: bacillus subtili]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:05 2008'' | ||
Revision as of 03:55, 31 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS PBP4A, AND ITS COMPLEX WITH A PEPTIDOGLYCAN MIMETIC PEPTIDE.
OverviewOverview
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.
About this StructureAbout this Structure
2J9P is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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