1o8h
From Proteopedia
(New page: 200px<br /> <applet load="1o8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o8h, resolution 2.20Å" /> '''PECTATE LYASE C FRO...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1O8H is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O8H OCA]]. | + | 1O8H is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O8H OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12540845 12540845] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12540845 12540845] | ||
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
| + | [[Category: Pectate lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Herron, S.R.]] | [[Category: Herron, S.R.]] | ||
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[[Category: pectate lyase cleavage]] | [[Category: pectate lyase cleavage]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:27:59 2007'' |
Revision as of 10:23, 30 October 2007
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PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 9.5 WITH 0.3MM CA2+ ADDED
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 ... [(full description)]
About this Structure
1O8H is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with CA as [ligand]. Active as [Pectate lyase], with EC number [4.2.2.2]. Structure known Active Site: AC1. 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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