1plu
From Proteopedia
(New page: 200px<br /><applet load="1plu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1plu, resolution 2.2Å" /> '''PECTATE LYASE C FROM ...) |
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| - | [[Image:1plu.gif|left|200px]]<br /><applet load="1plu" size=" | + | [[Image:1plu.gif|left|200px]]<br /><applet load="1plu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1plu, resolution 2.2Å" /> | caption="1plu, resolution 2.2Å" /> | ||
'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE'''<br /> | '''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI WITH 1 LU+3 ION IN THE PUTATIVE CALCIUM BINDING SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of pectate lyase C (EC 4.2.2.2) from the | + | 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== | ==About this Structure== | ||
| - | 1PLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with LU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1PLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with <scene name='pdbligand=LU:'>LU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jurnak, F | + | [[Category: Jurnak, F A.]] |
| - | [[Category: Yoder, M | + | [[Category: Yoder, M D.]] |
[[Category: LU]] | [[Category: LU]] | ||
[[Category: parallel beta-helix]] | [[Category: parallel beta-helix]] | ||
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[[Category: trans-elimination]] | [[Category: trans-elimination]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:11 2008'' |
Revision as of 12:30, 21 February 2008
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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 with as ligand. Active as Pectate lyase, with EC number 4.2.2.2 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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