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1pbi: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1pbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PBI FirstGlance]. <br>
<table><tr><td colspan='2'>[[1pbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PBI FirstGlance]. <br>
</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=1pbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbi OCA], [https://pdbe.org/1pbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pbi RCSB], [https://www.ebi.ac.uk/pdbsum/1pbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pbi ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#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=1pbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pbi OCA], [https://pdbe.org/1pbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pbi RCSB], [https://www.ebi.ac.uk/pdbsum/1pbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pbi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IBBB_PEA IBBB_PEA]] Inhibitor of trypsin and of chymotrypsin. May function as a natural phytochemical defense against predators.  
[https://www.uniprot.org/uniprot/IBBB_PEA IBBB_PEA] Inhibitor of trypsin and of chymotrypsin. May function as a natural phytochemical defense against predators.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1pbi ConSurf].
</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=1pbi ConSurf].
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== Publication Abstract from PubMed ==
The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are members of the Bowman-Birk protease inhibitor (BBPI) family. The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model. The inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit. Although the overall structure is very similar to that seen in other BBPIs, there are notable new structural features. Unlike the previously reported X-ray structures of BBPIs, the structure of PsTI-IVb includes the C-terminal segment of the molecule. The C-terminal tail of each subunit is partly beta-stranded and interacts with the 2-fold symmetry-related subunit, forming a beta-sheet with strands A and B of this subunit. The dimer is mainly stabilized by a large internal hydrogen-bonded network surrounded by two hydrophobic links. Fluorescence anisotropy decay measurements show that residues Tyr59 and Tyr43 are mobile in the picosecond time scale with a large amplitude. The fluorescence study and a molecular model of the simultaneous binding of PsTI-IVb to porcine trypsin and bovine chymotrypsin are compatible only with a monomeric state of the functional molecule in solution.
Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds.,Li de la Sierra I, Quillien L, Flecker P, Gueguen J, Brunie S J Mol Biol. 1999 Jan 22;285(3):1195-207. PMID:9887273<ref>PMID:9887273</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pbi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Pisum sativum]]
[[Category: Brunie, S]]
[[Category: Brunie S]]
[[Category: Sierra, I Li De La]]
[[Category: Li De La Sierra I]]
[[Category: Bowman-birk inhibitor]]
[[Category: Chymotrypsin inhibitor]]
[[Category: Trypsin inhibitor]]

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