1le7

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[[Image:1le7.gif|left|200px]]<br /><applet load="1le7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1le7.gif|left|200px]]
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caption="1le7, resolution 2.09&Aring;" />
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'''CARBOXYLIC ESTER HYDROLASE, C 2 2 21 space group'''<br />
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{{Structure
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|PDB= 1le7 |SIZE=350|CAPTION= <scene name='initialview01'>1le7</scene>, resolution 2.09&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]
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|GENE= PLA2GX10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''CARBOXYLIC ESTER HYDROLASE, C 2 2 21 space group'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE7 OCA].
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1LE7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE7 OCA].
==Reference==
==Reference==
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Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes., Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ, J Biol Chem. 2002 Aug 9;277(32):29086-93. Epub 2002 May 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12161451 12161451]
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Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes., Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ, J Biol Chem. 2002 Aug 9;277(32):29086-93. Epub 2002 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12161451 12161451]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: spla2-x]]
[[Category: spla2-x]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:53 2008''

Revision as of 10:29, 20 March 2008


PDB ID 1le7

Drag the structure with the mouse to rotate
, resolution 2.09Å
Ligands: and
Gene: PLA2GX10 (Homo sapiens)
Activity: Phospholipase A(2), with EC number 3.1.1.4
Coordinates: save as pdb, mmCIF, xml



CARBOXYLIC ESTER HYDROLASE, C 2 2 21 space group


Overview

The crystal structure of human group X (hGX) secreted phospholipase A2 (sPLA2) has been solved to a resolution of 1.97 A. As expected the protein fold is similar to previously reported sPLA2 structures. The active site architecture, including the positions of the catalytic residues and the first and second shell water around the Ca2+ cofactor, are highly conserved and remarkably similar to the group IB and group IIA enzymes. Differences are seen in the structures following the (1-12)-N-terminal helix and at the C terminus. These regions are proposed to interact with the substrate membrane surface. The opening to the active site slot is considerably larger in hGX than in human group IIA sPLA2. Furthermore, the electrostatic surface potential of the hGX interfacial-binding surface does not resemble that of the human group IIA sPLA2; the former is highly neutral, whereas the latter is highly cationic. The cationic residues on this face of group IB and IIA enzymes have been implicated in membrane binding and in k(cat*) allostery. In contrast, hGX does not show activation by the anionic charge at the lipid interface when acting on phospholipid vesicles or short-chain phospholipid micelles. Together, the crystal structure and kinetic results of hGX supports the conclusion that it is as active on zwitterionic as on anionic interfaces, and thus it is predicted to target the zwitterionic membrane surfaces of mammalian cells.

About this Structure

1LE7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes., Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ, J Biol Chem. 2002 Aug 9;277(32):29086-93. Epub 2002 May 25. PMID:12161451

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