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1plu
From Proteopedia
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|PDB= 1plu |SIZE=350|CAPTION= <scene name='initialview01'>1plu</scene>, resolution 2.2Å | |PDB= 1plu |SIZE=350|CAPTION= <scene name='initialview01'>1plu</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=LU:LUTETIUM (III) ION'>LU</scene> | + | |LIGAND= <scene name='pdbligand=LU:LUTETIUM+(III)+ION'>LU</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1plu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plu OCA], [http://www.ebi.ac.uk/pdbsum/1plu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1plu RCSB]</span> | ||
}} | }} | ||
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[[Category: Jurnak, F A.]] | [[Category: Jurnak, F A.]] | ||
[[Category: Yoder, M D.]] | [[Category: Yoder, M D.]] | ||
| - | [[Category: LU]] | ||
[[Category: parallel beta-helix]] | [[Category: parallel beta-helix]] | ||
[[Category: pectate cleavage]] | [[Category: pectate cleavage]] | ||
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[[Category: trans-elimination]] | [[Category: trans-elimination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:25 2008'' |
Revision as of 20:01, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE
Overview
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.
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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