2hp6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="2hp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hp6, resolution 2.20Å" /> '''Crystal structure of...
 
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2hp6.jpg|left|200px]]<br /><applet load="2hp6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2hp6, resolution 2.20&Aring;" />
'''Crystal structure of the OXA-10 W154A mutant at pH 7.5'''<br />


==About this Structure==
==Crystal structure of the OXA-10 W154A mutant at pH 7.5==
2HP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with SO4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HP6 OCA].  
<StructureSection load='2hp6' size='340' side='right'caption='[[2hp6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
[[Category: Beta-lactamase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[2hp6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HP6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hp6 OCA], [https://pdbe.org/2hp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hp6 RCSB], [https://www.ebi.ac.uk/pdbsum/2hp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hp6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLO10_PSEAI BLO10_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
== 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/hp/2hp6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2hp6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalytic efficiency of class D OXA-10 beta-lactamase depends critically on an unusual carboxylated lysine as the general base residue for both the enzyme acylation and deacylation steps of catalysis. Evidence is presented that the interaction between the indole group of Trp154 and the carboxylated lysine is essential for the stability of the post-translationally modified Lys70. Substitution of Trp154 by Gly, Ala or Phe yielded non carboxylated enzymes which displayed poor catalytic efficiencies and reduced stability when compared to the wild type OXA-10. The W154H mutant was partially carboxylated. In addition, the maximum values of kcat and kcat/KM were shifted toward pH 7 indicating that the carboxylation state of Lys70 is dependent on the protonation level of the histidine. A comparison of the three dimensional structures of the different proteins also indicated that the Trp154 mutations did not modify the overall structures of OXA-10 but induced an increased flexibility of the omega-loop in the active site. Finally, the deacylation impaired W154A mutant was used to determine the structure of the acyl-enzyme complex with benzylpenicillin. These results indicate a role of the Lys70 carboxylation during the deacylation step and emphasize the importance of Trp154 for the ideal positioning of active site residues leading to an optimum activity.
 
Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases.,Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F Biochemistry. 2009 Oct 27. PMID:19860471<ref>PMID:19860471</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hp6" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Charlier P]]
[[Category: Charlier, P.]]
[[Category: Falzone C]]
[[Category: Falzone, C.]]
[[Category: Herman R]]
[[Category: Herman, R.]]
[[Category: Kerff F]]
[[Category: Kerff, F.]]
[[Category: Sauvage E]]
[[Category: Sauvage, E.]]
[[Category: SO4]]
[[Category: class d beta-lactamase]]
[[Category: lysine carboxylation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:53:15 2007''

Latest revision as of 12:10, 6 November 2024

Crystal structure of the OXA-10 W154A mutant at pH 7.5Crystal structure of the OXA-10 W154A mutant at pH 7.5

Structural highlights

2hp6 is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLO10_PSEAI Hydrolyzes both carbenicillin and oxacillin.

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

The catalytic efficiency of class D OXA-10 beta-lactamase depends critically on an unusual carboxylated lysine as the general base residue for both the enzyme acylation and deacylation steps of catalysis. Evidence is presented that the interaction between the indole group of Trp154 and the carboxylated lysine is essential for the stability of the post-translationally modified Lys70. Substitution of Trp154 by Gly, Ala or Phe yielded non carboxylated enzymes which displayed poor catalytic efficiencies and reduced stability when compared to the wild type OXA-10. The W154H mutant was partially carboxylated. In addition, the maximum values of kcat and kcat/KM were shifted toward pH 7 indicating that the carboxylation state of Lys70 is dependent on the protonation level of the histidine. A comparison of the three dimensional structures of the different proteins also indicated that the Trp154 mutations did not modify the overall structures of OXA-10 but induced an increased flexibility of the omega-loop in the active site. Finally, the deacylation impaired W154A mutant was used to determine the structure of the acyl-enzyme complex with benzylpenicillin. These results indicate a role of the Lys70 carboxylation during the deacylation step and emphasize the importance of Trp154 for the ideal positioning of active site residues leading to an optimum activity.

Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases.,Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F Biochemistry. 2009 Oct 27. PMID:19860471[1]

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

See Also

References

  1. Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F. Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases. Biochemistry. 2009 Oct 27. PMID:19860471 doi:10.1021/bi901548c

2hp6, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA