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[[Image:1k9o.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX==
|PDB= 1k9o |SIZE=350|CAPTION= <scene name='initialview01'>1k9o</scene>, resolution 2.3&Aring;
<StructureSection load='1k9o' size='340' side='right'caption='[[1k9o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1k9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1i99 1i99]. The May 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Serpins''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_5 10.2210/rcsb_pdb/mom_2004_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K9O FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </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]] 2.3&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9o OCA], [https://pdbe.org/1k9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k9o RCSB], [https://www.ebi.ac.uk/pdbsum/1k9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k9o ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9o OCA], [http://www.ebi.ac.uk/pdbsum/1k9o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k9o RCSB]</span>
[https://www.uniprot.org/uniprot/SERA_MANSE SERA_MANSE] Inhibits elastase.
}}
== 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/k9/1k9o_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=1k9o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conformational changes are triggered in the serpin while maintaining the covalent linkage between the protease and serpin. Here we report the structure of a serpin-trypsin Michaelis complex, which we visualized by using the S195A trypsin mutant to prevent covalent complex formation. This encounter complex reveals a more extensive interaction surface than that present in small inhibitor-protease complexes and is a template for modeling other serpin-protease pairs. Mutations of several serpin residues at the interface reduced the inhibitory activity of the serpin. The serine residue C-terminal to the scissile peptide bond is found in a closer than usual interaction with His 57 at the active site of trypsin.


'''CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX'''
The structure of a Michaelis serpin-protease complex.,Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ Nat Struct Biol. 2001 Nov;8(11):979-83. PMID:11685246<ref>PMID:11685246</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1k9o" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conformational changes are triggered in the serpin while maintaining the covalent linkage between the protease and serpin. Here we report the structure of a serpin-trypsin Michaelis complex, which we visualized by using the S195A trypsin mutant to prevent covalent complex formation. This encounter complex reveals a more extensive interaction surface than that present in small inhibitor-protease complexes and is a template for modeling other serpin-protease pairs. Mutations of several serpin residues at the interface reduced the inhibitory activity of the serpin. The serine residue C-terminal to the scissile peptide bond is found in a closer than usual interaction with His 57 at the active site of trypsin.
*[[Serpin 3D structures|Serpin 3D structures]]
 
*[[Trypsin 3D structures|Trypsin 3D structures]]
==About this Structure==
== References ==
1K9O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Manduca_sexta Manduca sexta] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry 1I99. The following page contains interesting information on the relation of 1K9O with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb53_1.html Serpins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9O OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
The structure of a Michaelis serpin-protease complex., Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ, Nat Struct Biol. 2001 Nov;8(11):979-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11685246 11685246]
[[Category: Large Structures]]
[[Category: Manduca sexta]]
[[Category: Manduca sexta]]
[[Category: Protein complex]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Serpins]]
[[Category: Serpins]]
[[Category: Trypsin]]
[[Category: Belmares R]]
[[Category: Belmares, R.]]
[[Category: Bergstrom RC]]
[[Category: Bergstrom, R C.]]
[[Category: Cech AL]]
[[Category: Cech, A L.]]
[[Category: Corey DR]]
[[Category: Corey, D R.]]
[[Category: Goldsmith EJ]]
[[Category: Goldsmith, E J.]]
[[Category: Kanost MR]]
[[Category: Kanost, M R.]]
[[Category: Tong Y]]
[[Category: Tong, Y.]]
[[Category: Ye S]]
[[Category: Ye, S.]]
[[Category: michaelis serpin-protease complex inhibitory triad]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:25 2008''

Latest revision as of 11:54, 16 August 2023

CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEXCRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX

Structural highlights

1k9o is a 2 chain structure with sequence from Manduca sexta and Rattus norvegicus. This structure supersedes the now removed PDB entry 1i99. The May 2004 RCSB PDB Molecule of the Month feature on Serpins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SERA_MANSE Inhibits elastase.

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

Serine protease inhibitors (serpins) regulate the activities of circulating proteases. Serpins inhibit proteases by acylating the serine hydroxyl at their active sites. Before deacylation and complete proteolysis of the serpin can occur, massive conformational changes are triggered in the serpin while maintaining the covalent linkage between the protease and serpin. Here we report the structure of a serpin-trypsin Michaelis complex, which we visualized by using the S195A trypsin mutant to prevent covalent complex formation. This encounter complex reveals a more extensive interaction surface than that present in small inhibitor-protease complexes and is a template for modeling other serpin-protease pairs. Mutations of several serpin residues at the interface reduced the inhibitory activity of the serpin. The serine residue C-terminal to the scissile peptide bond is found in a closer than usual interaction with His 57 at the active site of trypsin.

The structure of a Michaelis serpin-protease complex.,Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ Nat Struct Biol. 2001 Nov;8(11):979-83. PMID:11685246[1]

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

See Also

References

  1. ↑ Ye S, Cech AL, Belmares R, Bergstrom RC, Tong Y, Corey DR, Kanost MR, Goldsmith EJ. The structure of a Michaelis serpin-protease complex. Nat Struct Biol. 2001 Nov;8(11):979-83. PMID:11685246 doi:10.1038/nsb1101-979

1k9o, resolution 2.30Å

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