1kge

From Proteopedia

(Difference between revisions)

Revision as of 07:44, 25 November 2020

STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT

Structural highlights

1kge is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	BLAZ ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885)
Activity:	Beta-lactamase, with EC number 3.5.2.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Two site-directed mutant enzymes of the class A beta-lactamase from Staphylococcus aureus PC1 were produced with the goal of blocking the site that in the native enzyme is occupied by the proposed hydrolytic water molecule. The crystal structures of these two mutant enzymes, N170Q and N170M, have been determined and refined at 2.2 and 2.0 A, respectively. They reveal that the side chain of Gln 170 displaces the water molecule, whereas that of Met170 does not. In both cases, the catalytic rates with benzylpenicillin are reduced by 10(4) compared with the native enzyme. With nitrocefin, the N170Q mutant enzyme exhibits an approximately 800-fold reduced rate compared with the native enzyme and in addition, a fast initial burst with stoichiometry of 1 mol of degraded nitrocefin/mol of enzyme. Stopped-flow kinetic experiments establish that the rate constant of the burst is 250 s-1, a value comparable with the rate of acylation of the native enzyme. Two structurally based mechanisms that explain the kinetic properties of the N170Q beta-lactamase are proposed, both invoking a deacylation-impaired enzyme due to the elimination of the hydrolytic water molecule. The catalytic rate of the N170M mutant enzyme with nitrocefin is reduced by approximately 50-fold compared with the native enzyme, and the slow progressive inhibition that is revealed indicates that the hydrolysis proceeds via a branched pathway mechanism. This is consistent with the structural data that show that the water site is preserved and that Met170 occupies part of the space that is required for substrate binding. The short contacts between the substrate and the enzyme may lead to structure perturbation and inactivation.

Elimination of the hydrolytic water molecule in a class A beta-lactamase mutant: crystal structure and kinetics.,Zawadzke LE, Chen CC, Banerjee S, Li Z, Wasch S, Kapadia G, Moult J, Herzberg O Biochemistry. 1996 Dec 24;35(51):16475-82. PMID:8987980^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zawadzke LE, Chen CC, Banerjee S, Li Z, Wasch S, Kapadia G, Moult J, Herzberg O. Elimination of the hydrolytic water molecule in a class A beta-lactamase mutant: crystal structure and kinetics. Biochemistry. 1996 Dec 24;35(51):16475-82. PMID:8987980 doi:10.1021/bi962242a

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kge"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT==
-<StructureSection load='1kge' size='340' side='right' caption='[[1kge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1kge' size='340' side='right'caption='[[1kge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kge]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KGE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kge]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KGE FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLAZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kge OCA], [http://pdbe.org/1kge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kge RCSB], [http://www.ebi.ac.uk/pdbsum/1kge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kge ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kge OCA], [http://pdbe.org/1kge PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kge RCSB], [http://www.ebi.ac.uk/pdbsum/1kge PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kge ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 12: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/1kge_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/1kge_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 27: @@
 </div>
 <div class="pdbe-citations 1kge" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 == References ==
 <references/>
@@ Line 32: / Line 35: @@
 </StructureSection>
 [[Category: Beta-lactamase]]
+[[Category: Large Structures]]
 [[Category: Chen, C C.H]]
 [[Category: Herzberg, O]]

1kge

From Proteopedia

Revision as of 07:44, 25 November 2020

STRUCTURE OF BETA-LACTAMASE ASN 170 MET MUTANT

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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