1yu6
From Proteopedia
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|PDB= 1yu6 |SIZE=350|CAPTION= <scene name='initialview01'>1yu6</scene>, resolution 1.55Å | |PDB= 1yu6 |SIZE=350|CAPTION= <scene name='initialview01'>1yu6</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu6 OCA], [http://www.ebi.ac.uk/pdbsum/1yu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yu6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Maynes, J T.]] | [[Category: Maynes, J T.]] | ||
[[Category: Qasim, M A.]] | [[Category: Qasim, M A.]] | ||
| - | [[Category: CA]] | ||
[[Category: protease]] | [[Category: protease]] | ||
[[Category: protein proteinase inhibitor]] | [[Category: protein proteinase inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:41 2008'' |
Revision as of 22:22, 30 March 2008
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| , resolution 1.55Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex
Overview
One of the most studied protein proteinase inhibitors is the turkey ovomucoid third domain, OMTKY3. This inhibitor contains a reactive-site loop (Lys13I-Arg21I) that binds in a nearly identical manner to all studied serine proteinases, regardless of their clan or specificity. The crystal structure of OMTKY3 bound to subtilisin Carlsberg (CARL) has been determined. There are two complete copies of the complexes in the crystallographic asymmetric unit. Whereas the two enzyme molecules are virtually identical [0.16 A root-mean-square difference (r.m.s.d.) for 274 C(alpha) atoms], the two inhibitor molecules show dramatic differences between one another (r.m.s.d. = 2.4 A for 50 C(alpha) atoms). When compared with other proteinase-bound OMTKY3 molecules, these inhibitors show even larger differences. This work facilitates a re-evaluation of the importance of certain ovomucoid residues in proteinase binding and explains why additivity and sequence-based binding-prediction methods fail for the CARL-OMTKY3 complex.
About this Structure
1YU6 is a Protein complex structure of sequences from Bacillus licheniformis and Meleagris gallopavo. Full crystallographic information is available from OCA.
Reference
Structure of the subtilisin Carlsberg-OMTKY3 complex reveals two different ovomucoid conformations., Maynes JT, Cherney MM, Qasim MA, Laskowski M Jr, James MN, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):580-8. Epub 2005, Apr 20. PMID:15858268
Page seeded by OCA on Mon Mar 31 01:22:41 2008
