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[[Image:1yu6.gif|left|200px]]


{{Structure
==Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex==
|PDB= 1yu6 |SIZE=350|CAPTION= <scene name='initialview01'>1yu6</scene>, resolution 1.55&Aring;
<StructureSection load='1yu6' size='340' side='right'caption='[[1yu6]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
<table><tr><td colspan='2'>[[1yu6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YU6 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yu6 OCA], [https://pdbe.org/1yu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yu6 RCSB], [https://www.ebi.ac.uk/pdbsum/1yu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yu6 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/IOVO_MELGA IOVO_MELGA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yu/1yu6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yu6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex'''
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<ref>PMID:15858268</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1yu6" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1YU6 is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU6 OCA].
__TOC__
 
</StructureSection>
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15858268 15858268]
[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
[[Category: Protein complex]]
[[Category: Cherney MM]]
[[Category: Subtilisin]]
[[Category: James MNG]]
[[Category: Cherney, M M.]]
[[Category: Laskowski Jr M]]
[[Category: James, M N.G.]]
[[Category: Maynes JT]]
[[Category: Jr., M Laskowski.]]
[[Category: Qasim MA]]
[[Category: Maynes, J T.]]
[[Category: Qasim, M A.]]
[[Category: protease]]
[[Category: protein proteinase inhibitor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:22:41 2008''

Latest revision as of 10:01, 23 August 2023

Crystal Structure of the Subtilisin Carlsberg:OMTKY3 ComplexCrystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex

Structural highlights

1yu6 is a 4 chain structure with sequence from Bacillus licheniformis and Meleagris gallopavo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IOVO_MELGA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Maynes JT, Cherney MM, Qasim MA, Laskowski M Jr, James MN. Structure of the subtilisin Carlsberg-OMTKY3 complex reveals two different ovomucoid conformations. Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):580-8. Epub 2005, Apr 20. PMID:15858268 doi:http://dx.doi.org/10.1107/S0907444905004889

1yu6, resolution 1.55Å

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