1bys
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The first crystal structure of a phospholipase D (PLD) family member has | + | The first crystal structure of a phospholipase D (PLD) family member has been determined at 2.0 A resolution. The PLD superfamily is defined by a common sequence motif, HxK(x)4D(x)6GSxN, and includes enzymes involved in signal transduction, lipid biosynthesis, endonucleases and open reading frames in pathogenic viruses and bacteria. The crystal structure suggests that residues from two sequence motifs form a single active site. A histidine residue from one motif acts as a nucleophile in the catalytic mechanism, forming a phosphoenzyme intermediate, whereas a histidine residue from the other motif appears to function as a general acid in the cleavage of the phosphodiester bond. The structure suggests that the conserved lysine residues are involved in phosphate binding. Large-scale genomic sequencing revealed that there are many PLD family members. Our results suggest that all of these proteins may possess a common structure and catalytic mechanism. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, J | + | [[Category: Dixon, J E.]] |
| - | [[Category: Stuckey, J | + | [[Category: Stuckey, J A.]] |
[[Category: WO4]] | [[Category: WO4]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: phosphodiesterase]] | [[Category: phosphodiesterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:36 2008'' |
Revision as of 10:00, 21 February 2008
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CRYSTAL STRUCTURE OF NUC COMPLEXED WITH TUNGSTATE
Overview
The first crystal structure of a phospholipase D (PLD) family member has been determined at 2.0 A resolution. The PLD superfamily is defined by a common sequence motif, HxK(x)4D(x)6GSxN, and includes enzymes involved in signal transduction, lipid biosynthesis, endonucleases and open reading frames in pathogenic viruses and bacteria. The crystal structure suggests that residues from two sequence motifs form a single active site. A histidine residue from one motif acts as a nucleophile in the catalytic mechanism, forming a phosphoenzyme intermediate, whereas a histidine residue from the other motif appears to function as a general acid in the cleavage of the phosphodiester bond. The structure suggests that the conserved lysine residues are involved in phosphate binding. Large-scale genomic sequencing revealed that there are many PLD family members. Our results suggest that all of these proteins may possess a common structure and catalytic mechanism.
About this Structure
1BYS is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of a phospholipase D family member., Stuckey JA, Dixon JE, Nat Struct Biol. 1999 Mar;6(3):278-84. PMID:10074947
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