1p5x
From Proteopedia
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|PDB= 1p5x |SIZE=350|CAPTION= <scene name='initialview01'>1p5x</scene>, resolution 2.0Å | |PDB= 1p5x |SIZE=350|CAPTION= <scene name='initialview01'>1p5x</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] </span> |
|GENE= PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | |GENE= PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ah7|1AH7]], [[1p6d|1P6D]], [[1p6e|1P6E]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5x OCA], [http://www.ebi.ac.uk/pdbsum/1p5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p5x RCSB]</span> | ||
}} | }} | ||
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[[Category: Monzingo, A F.]] | [[Category: Monzingo, A F.]] | ||
[[Category: Robertus, J D.]] | [[Category: Robertus, J D.]] | ||
| - | [[Category: ZN]] | ||
[[Category: tri zn2+ metal core]] | [[Category: tri zn2+ metal core]] | ||
| - | ''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 22:55:25 2008'' |
Revision as of 19:55, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Gene: | PLC (Bacillus cereus) | ||||||
| Activity: | Phospholipase C, with EC number 3.1.4.3 | ||||||
| Related: | 1AH7, 1P6D, 1P6E
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS
Overview
Because mutations of the ionizable Asp at position 55 of the phosphatidylcholine preferring phospholipase C from Bacillus cereus (PLC(Bc)) to a non-ionizable Asn generate a mutant enzyme (D55N) with 10(4)-fold lower catalytic activity than the wild-type enzyme, we tentatively identified Asp55 as the general base for the enzymatic reaction. To eliminate the alternate possibility that Asp55 is a structurally important amino acid, the X-ray structures of unbound D55N and complexes of D55N with two non-hydrolyzable substrate analogues have been solved and refined to 2.0, 2.0, and 2.3A, respectively. The structures of unbound wild-type PLC(Bc) and a wild-type PLC(Bc)-complex with a non-hydrolyzable substrate analogue do not change significantly as a result of replacing Asp55 with Asn. These observations demonstrate that Asp55 is not critical for the structural integrity of the enzyme and support the hypothesis that Asp55 is the general base in the PLC(Bc)-catalyzed hydrolysis of phospholipids.
About this Structure
1P5X is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base., Antikainen NM, Monzingo AF, Franklin CL, Robertus JD, Martin SF, Arch Biochem Biophys. 2003 Sep 1;417(1):81-6. PMID:12921783
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