2psp

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(New page: 200px<br /><applet load="2psp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2psp, resolution 1.9&Aring;" /> '''PORCINE PANCREATIC SP...)
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[[Image:2psp.jpg|left|200px]]<br /><applet load="2psp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2psp, resolution 1.9&Aring;" />
caption="2psp, resolution 1.9&Aring;" />
'''PORCINE PANCREATIC SPASMOLYTIC POLYPEPTIDE'''<br />
'''PORCINE PANCREATIC SPASMOLYTIC POLYPEPTIDE'''<br />
==Overview==
==Overview==
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The structure of a trigonal crystal form of porcine pancreatic spasmolytic, polypeptide (PSP) has been solved by molecular replacement and refined to, 1.95 A resolution. Three heavy-atom derivatives were prepared, giving, unbiased phase information, which was used in the model building of the, protein molecules. The final conventional R value is 19.8% with the, inclusion of 183 water molecules. PSP crystallizes as a dimer in space, group P3(1)21 with a non-crystallographic twofold axis relating the, monomers. The monomer consists of two very similar domains each composed, of three loop regions. Two clefts are found in the monomer, one in each, domain, that are proposed as possible substrate-binding sites. Important, interactions have been identified in the proposed substrate-binding sites, where conserved water molecules probably mimic the hydrophilic positions, of the substrate. The estimated cleft size is 9 x 9 x 12 A. Analysis of, the charge distribution within the clefts, by an electrostatic potential, calculation, shows the clefts to be essentially non-charged.
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The structure of a trigonal crystal form of porcine pancreatic spasmolytic polypeptide (PSP) has been solved by molecular replacement and refined to 1.95 A resolution. Three heavy-atom derivatives were prepared, giving unbiased phase information, which was used in the model building of the protein molecules. The final conventional R value is 19.8% with the inclusion of 183 water molecules. PSP crystallizes as a dimer in space group P3(1)21 with a non-crystallographic twofold axis relating the monomers. The monomer consists of two very similar domains each composed of three loop regions. Two clefts are found in the monomer, one in each domain, that are proposed as possible substrate-binding sites. Important interactions have been identified in the proposed substrate-binding sites, where conserved water molecules probably mimic the hydrophilic positions of the substrate. The estimated cleft size is 9 x 9 x 12 A. Analysis of the charge distribution within the clefts, by an electrostatic potential calculation, shows the clefts to be essentially non-charged.
==About this Structure==
==About this Structure==
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2PSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PSP OCA].
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2PSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PSP OCA].
==Reference==
==Reference==
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[[Category: Gajhede, M.]]
[[Category: Gajhede, M.]]
[[Category: Henriksen, A.]]
[[Category: Henriksen, A.]]
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[[Category: Petersen, T.N.]]
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[[Category: Petersen, T N.]]
[[Category: growth factor]]
[[Category: growth factor]]
[[Category: repeat]]
[[Category: repeat]]
[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:39:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:32:45 2008''

Revision as of 16:32, 21 February 2008


2psp, resolution 1.9Å

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PORCINE PANCREATIC SPASMOLYTIC POLYPEPTIDE

Overview

The structure of a trigonal crystal form of porcine pancreatic spasmolytic polypeptide (PSP) has been solved by molecular replacement and refined to 1.95 A resolution. Three heavy-atom derivatives were prepared, giving unbiased phase information, which was used in the model building of the protein molecules. The final conventional R value is 19.8% with the inclusion of 183 water molecules. PSP crystallizes as a dimer in space group P3(1)21 with a non-crystallographic twofold axis relating the monomers. The monomer consists of two very similar domains each composed of three loop regions. Two clefts are found in the monomer, one in each domain, that are proposed as possible substrate-binding sites. Important interactions have been identified in the proposed substrate-binding sites, where conserved water molecules probably mimic the hydrophilic positions of the substrate. The estimated cleft size is 9 x 9 x 12 A. Analysis of the charge distribution within the clefts, by an electrostatic potential calculation, shows the clefts to be essentially non-charged.

About this Structure

2PSP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Structure of porcine pancreatic spasmolytic polypeptide at 1.95 A resolution., Petersen TN, Henriksen A, Gajhede M, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):730-7. PMID:15299636

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