1yu6: Difference between revisions

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New page: left|200px<br /><applet load="1yu6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yu6, resolution 1.55Å" /> '''Crystal Structure of...
 
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[[Image:1yu6.gif|left|200px]]<br /><applet load="1yu6" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1yu6.gif|left|200px]]<br /><applet load="1yu6" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1yu6, resolution 1.55&Aring;" />
caption="1yu6, resolution 1.55&Aring;" />
'''Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex'''<br />
'''Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex'''<br />


==Overview==
==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.
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==
==About this Structure==
1YU6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YU6 OCA].  
1YU6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU6 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Cherney, M.M.]]
[[Category: Cherney, M M.]]
[[Category: James, M.N.G.]]
[[Category: James, M N.G.]]
[[Category: Jr., M.Laskowski.]]
[[Category: Jr., M Laskowski.]]
[[Category: Maynes, J.T.]]
[[Category: Maynes, J T.]]
[[Category: Qasim, M.A.]]
[[Category: Qasim, M A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: protease]]
[[Category: protease]]
[[Category: protein proteinase inhibitor]]
[[Category: protein proteinase inhibitor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:06 2008''

Revision as of 17:09, 21 February 2008

File:1yu6.gif


1yu6, resolution 1.55Å

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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 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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