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New page: left|200px<br /><applet load="1ppe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ppe, resolution 2.0Å" /> '''THE REFINED 2.0 ANGST...
 
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[[Image:1ppe.gif|left|200px]]<br /><applet load="1ppe" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ppe, resolution 2.0&Aring;" />
'''THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES'''<br />


==Overview==
==THE REFINED 2.0 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND CMTI-I, A TRYPSIN INHIBITOR FROM SQUASH SEEDS (CUCURBITA MAXIMA): TOPOLOGICAL SIMILARITY OF THE SQUASH SEED INHIBITORS WITH THE CARBOXYPEPTIDASE A INHIBITOR FROM POTATOES==
The stoichiometric complex formed between bovine beta-trypsin and the, Cucurbita maxima trypsin inhibitor I (CMTI-I) was crystallized and its, X-ray crystal structure determined using Patterson search techniques. Its, structure has been crystallographically refined to a final R value of, 0.152 (6.0-2.0 A). CMTI-I is of ellipsoidal shape; it lacks helices or, beta-sheets, but consists of turns and connecting short polypeptide, stretches. The disulfide pairing is CYS-3I-20I, Cys-10I-22I and, Cys-16I-28I. According to the polypeptide fold and disulfide connectivity, its structure resembles that of the carboxypeptidase A inhibitor from, potatoes. Thirteen of the 29 inhibitor residues are in direct contact with, trypsin; most of them are in the primary binding segment Val-2I, (P4)-Glu-9I (P4') which contains the reactive site bond Arg-5I-Ile-6I and, is in a conformation observed also for other serine proteinase inhibitors.
<StructureSection load='1ppe' size='340' side='right'caption='[[1ppe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ppe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PPE FirstGlance]. <br>
</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&#8491;</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=1ppe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ppe OCA], [https://pdbe.org/1ppe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ppe RCSB], [https://www.ebi.ac.uk/pdbsum/1ppe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ppe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
== 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/pp/1ppe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ppe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The stoichiometric complex formed between bovine beta-trypsin and the Cucurbita maxima trypsin inhibitor I (CMTI-I) was crystallized and its X-ray crystal structure determined using Patterson search techniques. Its structure has been crystallographically refined to a final R value of 0.152 (6.0-2.0 A). CMTI-I is of ellipsoidal shape; it lacks helices or beta-sheets, but consists of turns and connecting short polypeptide stretches. The disulfide pairing is CYS-3I-20I, Cys-10I-22I and Cys-16I-28I. According to the polypeptide fold and disulfide connectivity its structure resembles that of the carboxypeptidase A inhibitor from potatoes. Thirteen of the 29 inhibitor residues are in direct contact with trypsin; most of them are in the primary binding segment Val-2I (P4)-Glu-9I (P4') which contains the reactive site bond Arg-5I-Ile-6I and is in a conformation observed also for other serine proteinase inhibitors.


==About this Structure==
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.,Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T FEBS Lett. 1989 Jan 2;242(2):285-92. PMID:2914611<ref>PMID:2914611</ref>
1PPE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PPE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes., Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T, FEBS Lett. 1989 Jan 2;242(2):285-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2914611 2914611]
</div>
<div class="pdbe-citations 1ppe" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Trypsin 3D structures|Trypsin 3D structures]]
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Protein complex]]
[[Category: Cucurbita maxima]]
[[Category: Trypsin]]
[[Category: Large Structures]]
[[Category: Bode, W.]]
[[Category: Bode W]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: hydrolase(serine proteinase)]]
 
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