2g81: Difference between revisions

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-{{Seed}}
-[[Image:2g81.png|left|200px]]
-<!--
+==Crystal Structure of the Bowman-Birk Inhibitor from Vigna unguiculata Seeds in Complex with Beta-trypsin at 1.55 Angstrons Resolution==
-The line below this paragraph, containing "STRUCTURE_2g81", creates the "Structure Box" on the page.
+<StructureSection load='2g81' size='340' side='right'caption='[[2g81]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2g81]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Vigna_unguiculata Vigna unguiculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G81 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2g81|  PDB=2g81  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g81 OCA], [https://pdbe.org/2g81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g81 RCSB], [https://www.ebi.ac.uk/pdbsum/2g81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g81 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9S9H8_VIGUN Q9S9H8_VIGUN]
+== 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/g8/2g81_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=2g81 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure of the Bowman-Birk inhibitor from Vigna unguiculata seeds (BTCI) in complex with beta-trypsin was solved and refined at 1.55 A to a crystallographic R(factor) of 0.154 and R(free) of 0.169, and represents the highest resolution for a Bowman-Birk inhibitor structure to date. The BTCI-trypsin interface is stabilized by hydrophobic contacts and hydrogen bonds, involving two waters and a polyethylene glycol molecule. The conformational rigidity of the reactive loop is characteristic of the specificity against trypsin, while hydrophobicity and conformational mobility of the antichymotryptic subdomain confer the self-association tendency, indicated by atomic force microscopy, of BTCI in complex and free form. When BTCI is in binary complexes, no significant differences in inhibition constants for producing a ternary complex with trypsin and chymotrypsin were detected. These results indicate that binary complexes present no conformational change in their reactive site for both enzymes confirming that these sites are structurally independent. The free chymotrypsin observed in the atomic force microscopy assays, when the ternary complex is obtained from BTCI-trypsin binary complex and chymotrypsin, could be related more to the self-association tendency between chymotrypsin molecules and the flexibility of the reactive site for this enzyme than to binding-related conformational changes.
-===Crystal Structure of the Bowman-Birk Inhibitor from Vigna unguiculata Seeds in Complex with Beta-trypsin at 1.55 Angstrons Resolution===
+Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases.,Barbosa JA, Silva LP, Teles RC, Esteves GF, Azevedo RB, Ventura MM, de Freitas SM Biophys J. 2007 Mar 1;92(5):1638-50. Epub 2006 Dec 1. PMID:17142290<ref>PMID:17142290</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2g81" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17142290}}, adds the Publication Abstract to the page
+*[[Trypsin 3D structures|Trypsin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17142290 is the PubMed ID number.
+*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_17142290}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-G81 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Vigna_unguiculata Vigna unguiculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G81 OCA].
-==Reference==
-Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases., Barbosa JA, Silva LP, Teles RC, Esteves GF, Azevedo RB, Ventura MM, de Freitas SM, Biophys J. 2007 Mar 1;92(5):1638-50. Epub 2006 Dec 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17142290 17142290]
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Vigna unguiculata]]
-[[Category: Barbosa, J A.R G.]]
-[[Category: Esteves, G F.]]
-[[Category: Freitas, S M.]]
-[[Category: Paulino, L S.]]
-[[Category: Teles, R C.L.]]
-[[Category: Ventura, M M.]]
-[[Category: Bowman-birk inhibitor]]
-[[Category: Protein interaction]]
-[[Category: Protein self-association]]
-[[Category: Protein structure]]
-[[Category: Proteinase inhibitor]]
-[[Category: Serine proteinase]]
 [[Category: Vigna unguiculata]]
+[[Category: Barbosa JARG]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:37:20 2008''
+[[Category: Esteves GF]]
+[[Category: Freitas SM]]
+[[Category: Paulino LS]]
+[[Category: Teles RCL]]
+[[Category: Ventura MM]]