1hzo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hzo.jpg|left|200px]]<br /><applet load="1hzo" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1hzo.jpg|left|200px]]
-
caption="1hzo, resolution 1.75&Aring;" />
+
 
-
'''STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1'''<br />
+
{{Structure
 +
|PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75&Aring;
 +
|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==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1HZO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZO OCA].
+
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11916382 11916382]
+
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]]
Line 25: Line 34:
[[Category: mixed alpha/beta]]
[[Category: mixed alpha/beta]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:27 2008''
+
''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


PDB ID 1hzo

Drag the structure with the mouse to rotate
, 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

Page seeded by OCA on Thu Mar 20 11:43:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools