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1plu

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[[Image:1plu.gif|left|200px]]
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{{STRUCTURE_1plu| PDB=1plu | SCENE= }}
{{STRUCTURE_1plu| PDB=1plu | SCENE= }}
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'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE'''
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===PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE===
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==Overview==
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The crystal structure of pectate lyase C (EC 4.2.2.2) from the enterobacterium Erwinia chrysanthemi (PelC) has been refined by molecular dynamics techniques to a resolution of 2.2 A to an R factor of 17.97%. The final model consists of 352 of the total 353 amino acids and 114 solvent molecules. The root-mean-square deviation from ideality is 0.009 A for bond lengths and 1.768[deg] for bond angles. The structure of PelC bound to the lanthanide ion lutetium, used as a calcium analog, has also been refined. Lutetium inhibits the enzymatic activity of the protein, and in the PelC-lutetium structure, the ion binds in the putative calcium-binding site. Five side-chain atoms form ligands to the lutetium ion. An analysis of the atomic-level model of the two protein structures reveals possible implications for the enzymatic mechanism of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 12228363 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12228363}}
==About this Structure==
==About this Structure==
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[[Category: Pectinolytic activity]]
[[Category: Pectinolytic activity]]
[[Category: Trans-elimination]]
[[Category: Trans-elimination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:14:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:53:51 2008''

Revision as of 21:53, 28 July 2008

Template:STRUCTURE 1plu

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE

Template:ABSTRACT PUBMED 12228363

About this Structure

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

Reference

The Refined Three-Dimensional Structure of Pectate Lyase C from Erwinia chrysanthemi at 2.2 Angstrom Resolution (Implications for an Enzymatic Mechanism)., Yoder MD, Jurnak F, Plant Physiol. 1995 Feb;107(2):349-364. PMID:12228363

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