This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ct2

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:39, 14 July 2021

CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-THR18I IN COMPLEX WITH SGPB

Structural highlights

1ct2 is a 2 chain structure with sequence from Melga and Streptomyces griseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3sgb, 1sgr, 1sgq, 1sgp, 1cso, 1ct0, 1ct4
Activity:	Streptogrisin B, with EC number 3.4.21.81
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRTB_STRGR] Has a primary specificity for large aliphatic or aromatic amino acids.

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

Turkey ovomucoid third domain (OMTKY3) is a canonical inhibitor of serine proteinases. Upon complex formation, the inhibitors fully exposed P1 residue becomes fully buried in the preformed cavity of the enzyme. All 20 P1 variants of OMTKY3 have been obtained by recombinant DNA technology and their equilibrium association constants have been measured with six serine proteinases. To rationalize the trends observed in this data set, high resolution crystal structures have been determined for OMTKY3 P1 variants in complex with the bacterial serine proteinase, Streptomyces griseus proteinase B (SGPB). Four high resolution complex structures are being reported in this paper; the three beta-branched variants, Ile18I, Val18I, and Thr18I, determined to 2.1, 1.6, and 1.7 A resolution, respectively, and the structure of the Ser18I variant complex, determined to 1.9 A resolution. Models of the Cys18I, Hse18I, and Ape18I variant complexes are also discussed. The beta-branched side chains are not complementary to the shape of the S1 binding pocket in SGPB, in contrast to that of the wild-type gamma-branched P1 residue for OMTKY3, Leu18I. Chi1 angles of approximately 40 degrees are imposed on the side chains of Ile18I, Val18I, and Thr18I within the S1 pocket. Dihedral angles of +60 degrees, -60 degrees, or 180 degrees are more commonly observed but 40 degrees is not unfavorable for the beta-branched side chains. Thr18I Ogamma1 also forms a hydrogen bond with Ser195 Ogamma in this orientation. The Ser18I side chain adopts two alternate conformations within the S1 pocket of SGPB, suggesting that the side chain is not stable in either conformation.

Deleterious effects of beta-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB.,Bateman KS, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN Protein Sci. 2000 Jan;9(1):83-94. PMID:10739250^[1]

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

References

↑ Bateman KS, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN. Deleterious effects of beta-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB. Protein Sci. 2000 Jan;9(1):83-94. PMID:10739250

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ct2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ct2' size='340' side='right'caption='[[1ct2]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ct2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Melga Melga] and [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CT2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ct2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Melga Melga] and [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CT2 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sgb|3sgb]], [[1sgr|1sgr]], [[1sgq|1sgq]], [[1sgp|1sgp]], [[1cso|1cso]], [[1ct0|1ct0]], [[1ct4|1ct4]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sgb|3sgb]], [[1sgr|1sgr]], [[1sgq|1sgq]], [[1sgp|1sgp]], [[1cso|1cso]], [[1ct0|1ct0]], [[1ct4|1ct4]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Streptogrisin_B Streptogrisin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.81 3.4.21.81] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Streptogrisin_B Streptogrisin B], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.81 3.4.21.81] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ct2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct2 OCA], [http://pdbe.org/1ct2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ct2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ct2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct2 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ct2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct2 OCA], [https://pdbe.org/1ct2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ct2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ct2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PRTB_STRGR PRTB_STRGR]] Has a primary specificity for large aliphatic or aromatic amino acids.
+[[https://www.uniprot.org/uniprot/PRTB_STRGR PRTB_STRGR]] Has a primary specificity for large aliphatic or aromatic amino acids.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Proteinase|Proteinase]]
+*[[Proteinase 3D structures|Proteinase 3D structures]]
 == References ==
 <references/>

1ct2

From Proteopedia

Revision as of 10:39, 14 July 2021

CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-THR18I IN COMPLEX WITH SGPB

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox