1y9i
From Proteopedia
(New page: 200px<br /><applet load="1y9i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y9i, resolution 1.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:1y9i.jpg|left|200px]]<br /><applet load="1y9i" size=" | + | [[Image:1y9i.jpg|left|200px]]<br /><applet load="1y9i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y9i, resolution 1.8Å" /> | caption="1y9i, resolution 1.8Å" /> | ||
'''Crystal structure of low temperature requirement C protein from Listeria monocytogenes'''<br /> | '''Crystal structure of low temperature requirement C protein from Listeria monocytogenes'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphatidylglycerophosphatase (PGPase), an enzyme involved in lipid | + | 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== | ==About this Structure== | ||
| - | 1Y9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with CA, MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Y9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y9I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
[[Category: Kumaran, D.]] | [[Category: Kumaran, D.]] | ||
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
[[Category: Swaminathan, S.]] | [[Category: Swaminathan, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:07 2008'' |
Revision as of 14:03, 21 February 2008
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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 with , and as ligands. 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
Page seeded by OCA on Thu Feb 21 16:03:07 2008
Categories: Listeria monocytogenes | Single protein | Burley, S K. | Kumaran, D. | NYSGXRC, New York Structural GenomiX Research Consortium. | Swaminathan, S. | CA | GOL | MG | Helical bundle | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Putative pgpa | Structural genomics | Tetramer
