1g4i

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(New page: 200px<br /><applet load="1g4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4i, resolution 0.97&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g4i.jpg|left|200px]]<br /><applet load="1g4i" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g4i, resolution 0.97&Aring;" />
caption="1g4i, resolution 0.97&Aring;" />
'''CRYSTAL STRUCTURE OF THE BOVINE PANCREATIC PHOSPHOLIPASE A2 AT 0.97A'''<br />
'''CRYSTAL STRUCTURE OF THE BOVINE PANCREATIC PHOSPHOLIPASE A2 AT 0.97A'''<br />
==Overview==
==Overview==
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Using synchrotron radiation and a CCD camera, X-ray data have been, collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to, 0.97 A resolution allowing full anisotropic refinement. The final model, has a conventional R factor of 9.44% for all reflections, with a mean, standard uncertainty for the positional parameters of 0.031 A as, calculated from inversion of the full positional least-squares matrix. At, 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the, first time that its rigid scaffolding does not preclude flexibility, which, probably plays an important role in the catalytic process. Functionally, important regions (the interfacial binding site and calcium-binding loop), are located at the molecular surface, where conformational variability is, more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is, present at the entrance of the hydrophobic channel that leads to the, catalytic site and mimics the fatty-acid chains of a substrate analogue., Bovine pancreatic phospholipase A(2) at atomic resolution is compared with, previous crystallographic structures and with models derived from nuclear, magnetic resonance studies. Given the high structural similarity among, extracellular phospholipases A(2) observed so far at lower resolution, the, results arising from this structural analysis are expected to be of, general validity for this class of enzymes.
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Using synchrotron radiation and a CCD camera, X-ray data have been collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to 0.97 A resolution allowing full anisotropic refinement. The final model has a conventional R factor of 9.44% for all reflections, with a mean standard uncertainty for the positional parameters of 0.031 A as calculated from inversion of the full positional least-squares matrix. At 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the first time that its rigid scaffolding does not preclude flexibility, which probably plays an important role in the catalytic process. Functionally important regions (the interfacial binding site and calcium-binding loop) are located at the molecular surface, where conformational variability is more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is present at the entrance of the hydrophobic channel that leads to the catalytic site and mimics the fatty-acid chains of a substrate analogue. Bovine pancreatic phospholipase A(2) at atomic resolution is compared with previous crystallographic structures and with models derived from nuclear magnetic resonance studies. Given the high structural similarity among extracellular phospholipases A(2) observed so far at lower resolution, the results arising from this structural analysis are expected to be of general validity for this class of enzymes.
==About this Structure==
==About this Structure==
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1G4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA, CL, MRD and MPD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G4I OCA].
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1G4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MRD:'>MRD</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=1G4I OCA].
==Reference==
==Reference==
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[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra, B W.]]
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[[Category: Kalk, K.H.]]
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[[Category: Kalk, K H.]]
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[[Category: Murshudov, G.N.]]
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[[Category: Murshudov, G N.]]
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[[Category: Rozeboom, H.J.]]
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[[Category: Rozeboom, H J.]]
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[[Category: Steiner, R.A.]]
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[[Category: Steiner, R A.]]
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[[Category: Vries, A.de.]]
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[[Category: Vries, A de.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: CL]]
[[Category: CL]]
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[[Category: lipid degradation]]
[[Category: lipid degradation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:41:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:02 2008''

Revision as of 10:46, 21 February 2008


1g4i, resolution 0.97Å

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CRYSTAL STRUCTURE OF THE BOVINE PANCREATIC PHOSPHOLIPASE A2 AT 0.97A

Overview

Using synchrotron radiation and a CCD camera, X-ray data have been collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to 0.97 A resolution allowing full anisotropic refinement. The final model has a conventional R factor of 9.44% for all reflections, with a mean standard uncertainty for the positional parameters of 0.031 A as calculated from inversion of the full positional least-squares matrix. At 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the first time that its rigid scaffolding does not preclude flexibility, which probably plays an important role in the catalytic process. Functionally important regions (the interfacial binding site and calcium-binding loop) are located at the molecular surface, where conformational variability is more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is present at the entrance of the hydrophobic channel that leads to the catalytic site and mimics the fatty-acid chains of a substrate analogue. Bovine pancreatic phospholipase A(2) at atomic resolution is compared with previous crystallographic structures and with models derived from nuclear magnetic resonance studies. Given the high structural similarity among extracellular phospholipases A(2) observed so far at lower resolution, the results arising from this structural analysis are expected to be of general validity for this class of enzymes.

About this Structure

1G4I is a Single protein structure of sequence from Bos taurus with , , and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution., Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):516-26. PMID:11264580

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