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1o8d

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(New page: 200px<br /> <applet load="1o8d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o8d, resolution 2.20&Aring;" /> '''PECTATE LYASE C FRO...)
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==About this Structure==
==About this Structure==
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1O8D 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=1O8D OCA]].
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1O8D 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=1O8D 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]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:19:09 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:28:50 2007''

Revision as of 10:24, 30 October 2007


1o8d, resolution 2.20Å

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PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 11.2 WITH 5MM 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 ... [(full description)]

About this Structure

1O8D 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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