1byr
From Proteopedia
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| - | [[Image:1byr. | + | [[Image:1byr.jpg|left|200px]]<br /><applet load="1byr" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1byr" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1byr, resolution 2.0Å" /> | caption="1byr, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D FAMILY MEMBER, NUC FROM SALMONELLA TYPHIMURIUM'''<br /> | '''CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D FAMILY MEMBER, NUC FROM SALMONELLA TYPHIMURIUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BYR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. | + | 1BYR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Known structural/functional Site: <scene name='pdbsite=ACT:Residues From Both Monomers Create The Active Site'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BYR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phosphodiesterase]] | [[Category: phosphodiesterase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:36:12 2007'' |
Revision as of 12:26, 18 December 2007
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CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D FAMILY MEMBER, NUC FROM SALMONELLA TYPHIMURIUM
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
1BYR is a Single protein structure of sequence from Salmonella typhimurium. 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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