1cms
From Proteopedia
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| - | [[Image:1cms.gif|left|200px]] | + | [[Image:1cms.gif|left|200px]] |
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| - | '''THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cms |SIZE=350|CAPTION= <scene name='initialview01'>1cms</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chymosin Chymosin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.4 3.4.23.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CMS is a [ | + | 1CMS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMS OCA]. |
==Reference== | ==Reference== | ||
| - | The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution., Gilliland GL, Winborne EL, Nachman J, Wlodawer A, Proteins. 1990;8(1):82-101. PMID:[http:// | + | The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution., Gilliland GL, Winborne EL, Nachman J, Wlodawer A, Proteins. 1990;8(1):82-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2217166 2217166] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Chymosin]] | [[Category: Chymosin]] | ||
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[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
| - | ''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 10:26:17 2008'' |
Revision as of 08:26, 20 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Chymosin, with EC number 3.4.23.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION
Overview
The crystal structure of recombinant bovine chymosin (EC 3.4.23.4; renin), which was cloned and expressed in Escherichia coli, has been determined using X-ray data extending to 2.3 A resolution. The crystals of the enzyme used in this study belong to the space group I222 with unit cell dimensions alpha = 72.7 A, b = 80.3 A, and c = 114.8 A. The structure was solved by the molecular replacement method and was refined by a restrained least-squares procedure. The crystallographic R factor is 0.165 and the deviation of bond distances from ideality is 0.020 A. The resulting model includes all 323 amino acid residues, as well as 297 water molecules. The enzyme has an irregular shape with approximate maximum dimensions of 40 x 50 x 65 A. The secondary structure consists primarily of parallel and antiparallel beta-strands with a few short alpha-helices. The enzyme can be subdivided into N- and C-terminal domains which are separated by a deep cleft containing the active aspartate residues Asp-34 and Asp-216. The amino acid residues and waters at the active site form an extensive hydrogen-bonded network which maintains the pseudo 2-fold symmetry of the entire structure. A comparison of recombinant chymosin with other acid proteinases reveals the high degree of structural similarity with other members of this family of proteins as well as the subtle differences which make chymosin unique. In particular, Tyr-77 of the flap region of chymosin does not hydrogen bond to Trp-42 but protrudes out in the P1 pocket forming hydrophobic interactions with Phe-119 and Leu-32. This may have important implications concerning the mechanism of substrate binding and substrate specificity.
About this Structure
1CMS is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution., Gilliland GL, Winborne EL, Nachman J, Wlodawer A, Proteins. 1990;8(1):82-101. PMID:2217166
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