1yu6
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Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex
OverviewOverview
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 StructureAbout this Structure
1YU6 is a Protein complex structure of sequences from Bacillus licheniformis and Meleagris gallopavo with CA as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
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
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