1go8
From Proteopedia
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|PDB= 1go8 |SIZE=350|CAPTION= <scene name='initialview01'>1go8</scene>, resolution 2.00Å | |PDB= 1go8 |SIZE=350|CAPTION= <scene name='initialview01'>1go8</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+P'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+P'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1go8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1go8 OCA], [http://www.ebi.ac.uk/pdbsum/1go8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1go8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baumann, U.]] | [[Category: Baumann, U.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
[[Category: protease]] | [[Category: protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:04 2008'' |
Revision as of 17:48, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE METZINCIN'S METHIONINE: PRTC M226L MUTANT
Overview
Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.
About this Structure
1GO8 is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.
Reference
Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond., Hege T, Feltzer RE, Gray RD, Baumann U, J Biol Chem. 2001 Sep 14;276(37):35087-92. Epub 2001 Jul 9. PMID:11445573
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