1air: Difference between revisions

Revision as of 16:56, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1air.png

Template:STRUCTURE 1air

PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERSPECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS

Template:ABSTRACT PUBMED 12226275

About this StructureAbout this Structure

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

ReferenceReference

The Refined Three-Dimensional Structure of Pectate Lyase E from Erwinia chrysanthemi at 2.2 A Resolution., Lietzke SE, Scavetta RD, Yoder MD, Jurnak F, Plant Physiol. 1996 May;111(1):73-92. PMID:12226275

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OCA

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-'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS'''
+===PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS===
-==Overview==
+<!--
-The crystal structure of pectate lyase E (PelE; EC 4.2.2.2) from the enterobacteria Erwinia chrysanthemi has been refined by molecular dynamics techniques to a resolution of 2.2 A and an R factor (an agreement factor between observed structure factor amplitudes) of 16.1%. The final model consists of all 355 amino acids and 157 water molecules. The root-mean-square deviation from ideality is 0.009 A for bond lengths and 1.721[deg] for bond angles. The structure of PelE bound to a lanthanum ion, which inhibits the enzymatic activity, has also been refined and compared to the metal-free protein. In addition, the structures of pectate lyase C (PelC) in the presence and absence of a lutetium ion have been refined further using an improved algorithm for identifying waters and other solvent molecules. The two putative active site regions of PelE have been compared to those in the refined structure of PelC. The analysis of the atomic details of PelE and PelC in the presence and absence of lanthanide ions provides insight into the enzymatic mechanism of pectate lyases.
+The line below this paragraph, {{ABSTRACT_PUBMED_12226275}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12226275 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12226275}}
 ==About this Structure==
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 [[Category: Pectinolyitc activity]]
 [[Category: Trans-elimination]]
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