1hzo
From Proteopedia
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|PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75Å | |PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span> |
|GENE= BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 Proteus vulgaris]) | |GENE= BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 Proteus vulgaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzo OCA], [http://www.ebi.ac.uk/pdbsum/1hzo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hzo RCSB]</span> | ||
}} | }} | ||
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[[Category: Mayama, K.]] | [[Category: Mayama, K.]] | ||
[[Category: Nukaga, M.]] | [[Category: Nukaga, M.]] | ||
| - | [[Category: MES]] | ||
[[Category: cephalosporinase]] | [[Category: cephalosporinase]] | ||
[[Category: class a beta-lactamase]] | [[Category: class a beta-lactamase]] | ||
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[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:33 2008'' |
Revision as of 18:12, 30 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BLAC (Proteus vulgaris) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1
Overview
The structure of a chromosomal extended-spectrum beta-lactamase (ESBL) having the ability to hydrolyze cephalosporins including cefuroxime and ceftazidime has been determined by X-ray crystallography to 1.75 A resolution. The species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its structure solved by molecular replacement. Refinement of the model resulted in crystallographic R and R(free) of 16.9 % and 19.3 %, respectively. The folding of the K1 enzyme is broadly similar to that of non-ESBL TEM-type beta-lactamases (2 A rmsd for C(alpha)) and differs by only 0.35 A for all atoms of six conserved residues in the catalytic site. Other residues promoting extended-spectrum activity in K1 include the side-chains of atypical residues Ser237 and Lys276. These side-chains are linked by two water molecules, one of which lies in the position normally filled by the guanidinium group of Arg244, present in most non-ESBL enzymes but absent from K1. The ammonium group of Lys276, ca 3.5 A from the virtual Arg244 guanidinium position, may interact with polar R2 substitutents on the dihydrothiazene ring of cephalosporins.
About this Structure
1HZO is a Single protein structure of sequence from Proteus vulgaris. Full crystallographic information is available from OCA.
Reference
Structure of an extended-spectrum class A beta-lactamase from Proteus vulgaris K1., Nukaga M, Mayama K, Crichlow GV, Knox JR, J Mol Biol. 2002 Mar 15;317(1):109-17. PMID:11916382
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