1o8j: Difference between revisions

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[[Image:1o8j.jpg|left|200px]]
{{Seed}}
[[Image:1o8j.png|left|200px]]


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{{STRUCTURE_1o8j|  PDB=1o8j  |  SCENE=  }}  
{{STRUCTURE_1o8j|  PDB=1o8j  |  SCENE=  }}  


'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 4.5 WITH 30MM CA2+'''
===PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 4.5 WITH 30MM CA2+===




==Overview==
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Ca(2+) is essential for in vitro activity of Erwinia chrysanthemi pectate lyase C (PelC). Crystallographic analyses of 11 PelC-Ca(2+) complexes, formed at pH 4.5, 9.5, and 11.2 under varying Ca(2+) concentrations, have been solved and refined at a resolution of 2.2 A. The Ca(2+) site represents a new motif for Ca(2+), consisting primarily of beta-turns and beta-strands. The principal differences between PelC and the PelC-Ca(2+) structures at all pH values are the side-chain conformations of Asp-129 and Glu-166 as well as the occupancies of four water molecules. According to calculations of pK(a) values, the presence of Ca(2+) and associated structural changes lower the pK(a) of Arg-218, the amino acid responsible for proton abstraction during catalysis. The Ca(2+) affinity for PelC is weak, as the K(d) was estimated to be 0.132 (+/-0.004) mm at pH 9.5, 1.09 (+/-0.29) mm at pH 11.2, and 5.84 (+/-0.41) mm at pH 4.5 from x-ray diffraction studies and 0.133 (+/-0.045) mm at pH 9.5 from intrinsic tryptophan fluorescence measurements. Given the pH dependence of Ca(2+) affinity, PelC activity at pH 4.5 has been reexamined. At saturating Ca(2+) concentrations, PelC activity increases 10-fold at pH 4.5 but is less than 1% of maximal activity at pH 9.5. Taken together, the studies suggest that the primary Ca(2+) ion in PelC has multiple functions.
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{{ABSTRACT_PUBMED_12540845}}


==About this Structure==
==About this Structure==
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[[Category: Parallel beta-helix]]
[[Category: Parallel beta-helix]]
[[Category: Pectate lyase cleavage]]
[[Category: Pectate lyase cleavage]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:39:00 2008''

Revision as of 03:39, 28 July 2008

File:1o8j.png

Template:STRUCTURE 1o8j

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 4.5 WITH 30MM CA2+

Template:ABSTRACT PUBMED 12540845

About this Structure

1O8J is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.

Reference

Characterization and implications of Ca2+ binding to pectate lyase C., Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F, J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:12540845

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