1plu: Difference between revisions
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[[Image:1plu.gif|left|200px]] | [[Image:1plu.gif|left|200px]] | ||
'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE''' | {{Structure | ||
|PDB= 1plu |SIZE=350|CAPTION= <scene name='initialview01'>1plu</scene>, resolution 2.2Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PLU is a [ | 1PLU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLU OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12228363 12228363] | ||
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
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[[Category: trans-elimination]] | [[Category: trans-elimination]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:01 2008'' | ||
Revision as of 11:26, 20 March 2008
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| 1plu, resolution 2.2Å | |||||||||||||
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| Ligands: | LU | ||||||||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||||||||
| 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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