1hzo
From Proteopedia
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| - | [[Image:1hzo.jpg|left|200px]] | + | [[Image:1hzo.jpg|left|200px]] |
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| - | '''STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1''' | + | {{Structure |
| + | |PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 Proteus vulgaris]) | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HZO is a [ | + | 1HZO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11916382 11916382] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Proteus vulgaris]] | [[Category: Proteus vulgaris]] | ||
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[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:40 2008'' |
Revision as of 09:43, 20 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BLAC (Proteus vulgaris) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| 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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