1sib

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[[Image:1sib.gif|left|200px]]<br /><applet load="1sib" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sib.gif|left|200px]]
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caption="1sib, resolution 2.4&Aring;" />
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'''REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES'''<br />
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{{Structure
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|PDB= 1sib |SIZE=350|CAPTION= <scene name='initialview01'>1sib</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SIB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1SIB OCA].
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1SIB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SIB OCA].
==Reference==
==Reference==
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Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes., Heinz DW, Priestle JP, Rahuel J, Wilson KS, Grutter MG, J Mol Biol. 1991 Jan 20;217(2):353-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1992167 1992167]
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Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes., Heinz DW, Priestle JP, Rahuel J, Wilson KS, Grutter MG, J Mol Biol. 1991 Jan 20;217(2):353-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1992167 1992167]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
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[[Category: serine protease/inhibitor complex]]
[[Category: serine protease/inhibitor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:19 2008''

Revision as of 12:05, 20 March 2008


PDB ID 1sib

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Activity: Subtilisin, with EC number 3.4.21.62
Coordinates: save as pdb, mmCIF, xml



REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES


Overview

The crystal structures of the complexes formed between subtilisin Novo and three inhibitors, eglin c, Arg45-eglin c and Lys53-eglin c have been determined using molecular replacement and difference Fourier techniques and refined at 2.4 A, 2.1 A, and 2.4 A resolution, respectively. The mutants Arg45-eglin c and Lys53-eglin c were constructed by site-directed mutagenesis in order to investigate the inhibitory specificity and stability of eglin c. Arg45-eglin became a potent trypsin inhibitor, in contrast to native eglin, which is an elastase inhibitor. This specificity change was rationalized by comparing the structures of Arg45-eglin and basic pancreatic trypsin inhibitor and their interactions with trypsin. The residue Arg53, which participates in a complex network of hydrogen bonds formed between the core and the binding loop of eglin c, was replaced with the shorter basic amino acid lysine in the mutant Lys53-eglin. Two hydrogen bonds with Thr44, located in the binding loop, can no longer be formed but are partially restored by a water molecule bound in the vicinity of Lys53. Eglin c in complexes with both subtilisin Novo and subtilisin Carlsberg was crystallized in two different space groups. Comparison of the complexes showed a rigid body rotation for the eglin c core of 11.5 degrees with respect to the enzyme, probably caused by different intermolecular contacts in both crystal forms.

About this Structure

1SIB is a Protein complex structure of sequences from Bacillus subtilis and Hirudo medicinalis. Full crystallographic information is available from OCA.

Reference

Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes., Heinz DW, Priestle JP, Rahuel J, Wilson KS, Grutter MG, J Mol Biol. 1991 Jan 20;217(2):353-71. PMID:1992167

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