1o8j: Difference between revisions
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'''PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 4.5 WITH 30MM CA2+''' | {{Structure | ||
|PDB= 1o8j |SIZE=350|CAPTION= <scene name='initialview01'>1o8j</scene>, resolution 2.20Å | |||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</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 AT PH 4.5 WITH 30MM CA2+''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1O8J is a [ | 1O8J 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=1O8J OCA]. | ||
==Reference== | ==Reference== | ||
Characterization and implications of Ca2+ binding to pectate lyase C., Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F, J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:[http:// | Characterization and implications of Ca2+ binding to pectate lyase C., Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F, J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12540845 12540845] | ||
[[Category: Erwinia chrysanthemi]] | [[Category: Erwinia chrysanthemi]] | ||
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
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[[Category: pectate lyase cleavage]] | [[Category: pectate lyase cleavage]] | ||
''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 13:07:14 2008'' | ||
Revision as of 11:07, 20 March 2008
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| 1o8j, resolution 2.20Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | CA | ||||||||||||
| Activity: | Pectate lyase, with EC number 4.2.2.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT PH 4.5 WITH 30MM CA2+
Overview
Ca(2+) is essential for in vitro activity of Erwinia chrysanthemi pectate lyase C (PelC). Crystallographic analyses of 11 PelC-Ca(2+) complexes, formed at pH 4.5, 9.5, and 11.2 under varying Ca(2+) concentrations, have been solved and refined at a resolution of 2.2 A. The Ca(2+) site represents a new motif for Ca(2+), consisting primarily of beta-turns and beta-strands. The principal differences between PelC and the PelC-Ca(2+) structures at all pH values are the side-chain conformations of Asp-129 and Glu-166 as well as the occupancies of four water molecules. According to calculations of pK(a) values, the presence of Ca(2+) and associated structural changes lower the pK(a) of Arg-218, the amino acid responsible for proton abstraction during catalysis. The Ca(2+) affinity for PelC is weak, as the K(d) was estimated to be 0.132 (+/-0.004) mm at pH 9.5, 1.09 (+/-0.29) mm at pH 11.2, and 5.84 (+/-0.41) mm at pH 4.5 from x-ray diffraction studies and 0.133 (+/-0.045) mm at pH 9.5 from intrinsic tryptophan fluorescence measurements. Given the pH dependence of Ca(2+) affinity, PelC activity at pH 4.5 has been reexamined. At saturating Ca(2+) concentrations, PelC activity increases 10-fold at pH 4.5 but is less than 1% of maximal activity at pH 9.5. Taken together, the studies suggest that the primary Ca(2+) ion in PelC has multiple functions.
About this Structure
1O8J is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
Reference
Characterization and implications of Ca2+ binding to pectate lyase C., Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F, J Biol Chem. 2003 Apr 4;278(14):12271-7. Epub 2003 Jan 22. PMID:12540845
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