1air
From Proteopedia
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| - | [[Image:1air.gif|left|200px]] | + | [[Image:1air.gif|left|200px]] |
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| - | '''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS''' | + | {{Structure |
| + | |PDB= 1air |SIZE=350|CAPTION= <scene name='initialview01'>1air</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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 (EC16) TO A RESOLUTION OF 2.2 ANGSTROMS WITH 128 WATERS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AIR is a [ | + | 1AIR 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=1AIR OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12226275 12226275] |
[[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 09:58:08 2008'' |
Revision as of 07:58, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1AIR 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 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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