1sup
From Proteopedia
(New page: 200px<br /><applet load="1sup" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sup, resolution 1.6Å" /> '''SUBTILISIN BPN' AT 1....) |
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| - | [[Image:1sup.jpg|left|200px]]<br /><applet load="1sup" size=" | + | [[Image:1sup.jpg|left|200px]]<br /><applet load="1sup" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sup, resolution 1.6Å" /> | caption="1sup, resolution 1.6Å" /> | ||
'''SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS'''<br /> | '''SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the serine protease subtilisin BPN' | + | The three-dimensional structure of the serine protease subtilisin BPN' (SBT) has been refined at 1.6 A resolution in space group C2 to a final R value of 0.17. 17 regions of discrete disorder have been identified and analyzed. Two of these are dual-conformation peptide units; the remainder involve alternate rotamers of side chains either alone or in small clusters. The structure is compared with previously reported high-resolution models of SBT in two other space groups, P2(1)2(1)2(1) and P2(1). Apart from the surface, there are no significant variations in structure among the three crystal forms. Structural variations observed at the protein surface occur predominantly in regions of protein-protein contact. The crystal packing arrangements in the three space groups are compared. |
==About this Structure== | ==About this Structure== | ||
| - | 1SUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with CA, NA and PMS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http:// | + | 1SUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=PMS:'>PMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
[[Category: Betzel, C.]] | [[Category: Betzel, C.]] | ||
| - | [[Category: Gallagher, D | + | [[Category: Gallagher, D T.]] |
| - | [[Category: Gilliland, G | + | [[Category: Gilliland, G L.]] |
| - | [[Category: Oliver, J | + | [[Category: Oliver, J D.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: NA]] | [[Category: NA]] | ||
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[[Category: hydrolase (serine protease)]] | [[Category: hydrolase (serine protease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:23 2008'' |
Revision as of 13:05, 21 February 2008
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SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS
Overview
The three-dimensional structure of the serine protease subtilisin BPN' (SBT) has been refined at 1.6 A resolution in space group C2 to a final R value of 0.17. 17 regions of discrete disorder have been identified and analyzed. Two of these are dual-conformation peptide units; the remainder involve alternate rotamers of side chains either alone or in small clusters. The structure is compared with previously reported high-resolution models of SBT in two other space groups, P2(1)2(1)2(1) and P2(1). Apart from the surface, there are no significant variations in structure among the three crystal forms. Structural variations observed at the protein surface occur predominantly in regions of protein-protein contact. The crystal packing arrangements in the three space groups are compared.
About this Structure
1SUP is a Single protein structure of sequence from Bacillus amyloliquefaciens with , and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
Subtilisin BPN' at 1.6 A resolution: analysis for discrete disorder and comparison of crystal forms., Gallagher T, Oliver J, Bott R, Betzel C, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1125-35. PMID:15299573
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