This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1o88

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o88.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1o88.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o88| PDB=1o88 | SCENE= }}
{{STRUCTURE_1o88| PDB=1o88 | SCENE= }}
-
'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 11.2 WITH 30MM CA2+'''
+
===PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 11.2 WITH 30MM CA2+===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12540845}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12540845 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12540845}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Parallel beta-helix]]
[[Category: Parallel beta-helix]]
[[Category: Pectate lyase cleavage]]
[[Category: Pectate lyase cleavage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:30:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:45:57 2008''

Revision as of 04:45, 28 July 2008

Image:1o88.png

Template:STRUCTURE 1o88

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 11.2 WITH 30MM CA2+

Template:ABSTRACT PUBMED 12540845

About this Structure

1O88 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

Page seeded by OCA on Mon Jul 28 07:45:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o88"
Personal tools