1y9i

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|PDB= 1y9i |SIZE=350|CAPTION= <scene name='initialview01'>1y9i</scene>, resolution 1.8&Aring;
|PDB= 1y9i |SIZE=350|CAPTION= <scene name='initialview01'>1y9i</scene>, resolution 1.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1267 PgpA]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9i OCA], [http://www.ebi.ac.uk/pdbsum/1y9i PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1y9i RCSB]</span>
}}
}}
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan, S.]]
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[[Category: CA]]
 
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[[Category: GOL]]
 
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[[Category: MG]]
 
[[Category: helical bundle]]
[[Category: helical bundle]]
[[Category: new york structural genomix research consortium]]
[[Category: new york structural genomix research consortium]]
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[[Category: tetramer]]
[[Category: tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:14:14 2008''

Revision as of 04:14, 26 March 2008


PDB ID 1y9i

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: , , ,
Domains: PgpA
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of low temperature requirement C protein from Listeria monocytogenes


Overview

Phosphatidylglycerophosphatase (PGPase), an enzyme involved in lipid metabolism, catalyzes formation of phosphatidylglycerol from phosphatidylglycerophosphate. Phosphatidylglycerol is a multifunctional phospholipid, found in the biological membranes of many organisms. Here, we report the crystal structure of Listeria monocytogenes PGPase at 1.8 A resolution. PGPase, an all-helical molecule, forms a homotetramer. Each protomer contains an independent active site with two metal ions, Ca(2+) and Mg(2+), forming a hetero-binuclear center located in a hydrophilic cavity near the surface of the molecule. The binuclear center, conserved ligands, metal-bound water molecules, and an Asp-His dyad form the active site. The catalytic mechanism of this enzyme is likely to proceed via binuclear metal activated nucleophilic water. The binuclear metal-binding active-site environment of this structure should provide insights into substrate binding and metal-dependent catalysis. A long channel with inter-linked linear water chains, termed "proton wires," is observed at the tetramer interface. Comparison of similar water chain structures in photosynthetic reaction centers (RCs), Cytochrome f, gramicidin, and bacteriorhodopsin, suggests that PGPase may conduct protons via proton wires.

About this Structure

1Y9I is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two "proton wires"., Kumaran D, Bonanno JB, Burley SK, Swaminathan S, Proteins. 2006 Sep 1;64(4):851-62. PMID:16838328

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