1hzo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:18, 9 August 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hzo.jpg|left|200px]]
 
-
{{Structure
+
==STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1==
-
|PDB= 1hzo |SIZE=350|CAPTION= <scene name='initialview01'>1hzo</scene>, resolution 1.75&Aring;
+
<StructureSection load='1hzo' size='340' side='right'caption='[[1hzo]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>
+
<table><tr><td colspan='2'>[[1hzo]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZO FirstGlance]. <br>
-
|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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-
|GENE= BLAC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 Proteus vulgaris])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hzo OCA], [https://pdbe.org/1hzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hzo RCSB], [https://www.ebi.ac.uk/pdbsum/1hzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hzo ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|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>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/BLAB_PROVU BLAB_PROVU] Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefuroxime and cefotaxime.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/1hzo_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hzo ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1'''
+
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<ref>PMID:11916382</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1hzo" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
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].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
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: Proteus vulgaris]]
[[Category: Proteus vulgaris]]
-
[[Category: Single protein]]
+
[[Category: Crichlow GV]]
-
[[Category: Crichlow, G V.]]
+
[[Category: Knox JR]]
-
[[Category: Knox, J R.]]
+
[[Category: Kuzin AP]]
-
[[Category: Kuzin, A P.]]
+
[[Category: Mayama K]]
-
[[Category: Mayama, K.]]
+
[[Category: Nukaga M]]
-
[[Category: Nukaga, M.]]
+
-
[[Category: cephalosporinase]]
+
-
[[Category: class a beta-lactamase]]
+
-
[[Category: hydrolase]]
+
-
[[Category: mixed alpha/beta]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:33 2008''
+

Current revision

STRUCTURE OF CLASS A CEPHALOSPORINASE FROM PROTEUS VULGARIS K1

PDB ID 1hzo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hzo"
Personal tools