1omj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1omj.jpg|left|200px]]
{{Seed}}
[[Image:1omj.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1omj|  PDB=1omj  |  SCENE=  }}  
{{STRUCTURE_1omj|  PDB=1omj  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18'''
===CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18===




==Overview==
<!--
The psychrophilic alkaline metalloprotease (PAP) produced by a Pseudomonas bacterium isolated in Antarctica belongs to the clan of metzincins, for which a zinc ion is essential for catalytic activity. Binding studies in the crystalline state have been performed by X-ray crystallography in order to improve the understanding of the role of the zinc and calcium ions bound to this protease. Cocrystallization and soaking experiments with EDTA in a concentration range from 1 to 85 mM have resulted in five three-dimensional structures with a distinct number of metal ions occupying the ion-binding sites. Evolution of the structural changes observed in the vicinity of each cation-binding site has been studied as a function of the concentration of EDTA, as well as of time, in the presence of the chelator. Among others, we have found that the catalytic zinc ion was the first ion to be chelated, ahead of a weakly bound calcium ion (Ca 700) exclusive to the psychrophilic enzyme. Upon removal of the catalytic zinc ion, the side chains of the active-site residues His-173, His-179 and Tyr-209 shifted approximately 4, 1.0, and 1.6 A, respectively. Our studies confirm and also explain the sensitivity of PAP toward moderate EDTA concentrations and propose distinct roles for the calcium ions. A new crystal form of native PAP validates our previous predictions regarding the adaptation of this enzyme to cold environments as well as the proteolytic domain calcium ion being exclusive for PAP independent of crystallization conditions.
The line below this paragraph, {{ABSTRACT_PUBMED_12837794}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12837794 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12837794}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Ravaud, S.]]
[[Category: Ravaud, S.]]
[[Category: Beta jelly roll]]
[[Category: Beta jelly roll]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:01:58 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:18:25 2008''

Revision as of 05:18, 28 July 2008

File:1omj.png

Template:STRUCTURE 1omj

CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18

Template:ABSTRACT PUBMED 12837794

About this Structure

1OMJ is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography., Ravaud S, Gouet P, Haser R, Aghajari N, J Bacteriol. 2003 Jul;185(14):4195-203. PMID:12837794

Page seeded by OCA on Mon Jul 28 08:18:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1omj&oldid=689562"