1esp
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1esp.jpg|left|200px]] | + | [[Image:1esp.jpg|left|200px]] |
| - | + | ||
| - | '''NEUTRAL PROTEASE MUTANT E144S''' | + | {{Structure |
| + | |PDB= 1esp |SIZE=350|CAPTION= <scene name='initialview01'>1esp</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CNP (GENBANK ACCESSION #M83910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | ||
| + | }} | ||
| + | |||
| + | '''NEUTRAL PROTEASE MUTANT E144S''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1ESP is a [ | + | 1ESP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESP OCA]. |
==Reference== | ==Reference== | ||
| - | E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution., Lister SA, Wetmore DR, Roche RS, Codding PW, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):543-50. PMID:[http:// | + | E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution., Lister SA, Wetmore DR, Roche RS, Codding PW, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):543-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299677 15299677] |
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 19: | Line 28: | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| - | [[Category: inactive mutant | + | [[Category: inactive mutant e144]] |
| - | ''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 10:59:47 2008'' |
Revision as of 08:59, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | CNP (GENBANK ACCESSION #M83910 (Bacillus cereus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NEUTRAL PROTEASE MUTANT E144S
Overview
The X-ray crystal structure of the Bacillus cereus neutral protease (CNP) active-site mutant E144S, in which the putative general base proposed for the thermolysin-like zinc neutral proteases, Glu144, has been replaced by serine, has been determined to a resolution of 2.8 A. This represents the first crystal structure of an active-site mutant of a zinc neutral protease. The E 144S mutant was crystallized in the hexagonal space group, P6(5)22, with unit-cell dimensions a = b = 76.57, c = 201.91 A. Although the ligands involved in zinc coordination in the active site are identical to those found in the wild-type protein, the mutation results in a modified environment around the zinc ion; particularly with respect to the water molecules. While the structure of the mutant is similar to that of wild type, its protease activity is reduced to 0.16% that of the wild-type CNP and the protein is virtually resistant to autolysis in the presence of calcium. The lowered protease activity of the mutant is consistent with the role proposed for Glu144 as the general base in the catalysis of thermolysin-like neutral proteases [Matthews (1988). Acc. Chem. Res. 21, 333-340]. We suggest that the residual activity of the E144S mutant arises from a water molecule, which is found within hydrogen-bonding distance of Ser144, acting as a general base in the catalytic function of the mutant.
About this Structure
1ESP is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution., Lister SA, Wetmore DR, Roche RS, Codding PW, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):543-50. PMID:15299677
Page seeded by OCA on Thu Mar 20 10:59:47 2008
