1nsa
From Proteopedia
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| - | [[Image:1nsa.gif|left|200px]] | + | [[Image:1nsa.gif|left|200px]] |
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| - | '''THREE-DIMENSIONAL STRUCTURE OF PORCINE PROCARBOXYPEPTIDASE B: A STRUCTURAL BASIS OF ITS INACTIVITY''' | + | {{Structure |
| + | |PDB= 1nsa |SIZE=350|CAPTION= <scene name='initialview01'>1nsa</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF PORCINE PROCARBOXYPEPTIDASE B: A STRUCTURAL BASIS OF ITS INACTIVITY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NSA is a [ | + | 1NSA is a [[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=1NSA OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity., Coll M, Guasch A, Aviles FX, Huber R, EMBO J. 1991 Jan;10(1):1-9. PMID:[http:// | + | Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity., Coll M, Guasch A, Aviles FX, Huber R, EMBO J. 1991 Jan;10(1):1-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1989878 1989878] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:00 2008'' |
Revision as of 11:01, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF PORCINE PROCARBOXYPEPTIDASE B: A STRUCTURAL BASIS OF ITS INACTIVITY
Overview
Procarboxypeptidase B is converted to enzymatically active carboxypeptidase B by limited proteolysis catalysed by trypsin, removing the long N-terminal activation segment of 95 amino acids. The three-dimensional crystal structure of procarboxypeptidase B from porcine pancreas has been determined at 2.3 A resolution and refined to a crystallographic R-factor of 0.169. The functional determinants of its enzymatic inactivity and of its activation by limited proteolysis have thus been unveiled. The activation segment folds in a globular region with an open sandwich antiparallel-alpha antiparallel-beta topology and in a C terminal alpha-helix which connects it to the enzyme moiety. The globular region (A7-A82) shields the preformed active site, and establishes specific interactions with residues important for substrate recognition. AspA41 forms a salt bridge with Arg145, which in active carboxypeptidase binds the C-terminal carboxyl group of substrate molecules. The connecting region occupies the putative extended substrate binding site. The scissile peptide bond cleaved by trypsin during activation is very exposed. Its cleavage leads to the release of the activation segment and to exposure of the substrate binding site. An open-sandwich folding has been observed in a number of other proteins and protein domains. One of them is the C-terminal fragment of L7/L12, a ribosomal protein from Escherichia coli that displays a topology similar to the activation domain of procarboxypeptidase.
About this Structure
1NSA is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity., Coll M, Guasch A, Aviles FX, Huber R, EMBO J. 1991 Jan;10(1):1-9. PMID:1989878
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