1g9i: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (12 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF BETA-TRYSIN COMPLEX IN CYCLOHEXANE== | |||
<StructureSection load='1g9i' size='340' side='right'caption='[[1g9i]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1g9i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Vigna_radiata_var._radiata Vigna radiata var. radiata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G9I 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]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1g9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g9i OCA], [https://pdbe.org/1g9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g9i RCSB], [https://www.ebi.ac.uk/pdbsum/1g9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g9i 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/g9/1g9i_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=1g9i ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The active trypsin inhibiting component, SPC1, was obtained during the synthesis of a 22-residue peptide with three disulfide bridges according to the mimic mung bean Bowman-Birk type inhibitor. The K(i) value of SPC1 is 1.2x10(-7) M. In order to determine the topological structure of SPC1, X-ray diffraction studies were carried out on the complex of SPC1 with bovine beta-trypsin. Only the binding loop of SPC1 resolved at 2.2 A resolution due to conformational flexibility of the other residues [1]. The amino acid sequence was re-determined and electrospray mass spectroscopy was also performed to ensure that no cleaving occurred on SPC1 and the primary sequence of SPC1 is correct. Because the protein is more rigid in nonaqueous medium as has been proved by others [2], we treated the complex of SPC1 with neat cyclohexane and then subjected it to X-ray diffraction analysis, and the result showed that all the 22 residues of SPC1 were located in the electron density map. So the topological structure of SPC1 has been determined, suggesting that crystal treatment with cyclohexane may be used as a method to determine the conformation of the disordered regions in protein crystal structures. | |||
X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane.,Zhu G, Huang Q, Zhu Y, Li Y, Chi C, Tang Y Biochim Biophys Acta. 2001 Mar 9;1546(1):98-106. PMID:11257512<ref>PMID:11257512</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1g9i" 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: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vigna radiata var. radiata]] | ||
[[Category: Chi | [[Category: Chi C]] | ||
[[Category: Huang | [[Category: Huang Q]] | ||
[[Category: Li | [[Category: Li Y]] | ||
[[Category: Tang | [[Category: Tang Y]] | ||
[[Category: Zhu | [[Category: Zhu G]] | ||
[[Category: Zhu | [[Category: Zhu Y]] | ||
Latest revision as of 09:10, 9 August 2023
CRYSTAL STRUCTURE OF BETA-TRYSIN COMPLEX IN CYCLOHEXANECRYSTAL STRUCTURE OF BETA-TRYSIN COMPLEX IN CYCLOHEXANE
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe active trypsin inhibiting component, SPC1, was obtained during the synthesis of a 22-residue peptide with three disulfide bridges according to the mimic mung bean Bowman-Birk type inhibitor. The K(i) value of SPC1 is 1.2x10(-7) M. In order to determine the topological structure of SPC1, X-ray diffraction studies were carried out on the complex of SPC1 with bovine beta-trypsin. Only the binding loop of SPC1 resolved at 2.2 A resolution due to conformational flexibility of the other residues [1]. The amino acid sequence was re-determined and electrospray mass spectroscopy was also performed to ensure that no cleaving occurred on SPC1 and the primary sequence of SPC1 is correct. Because the protein is more rigid in nonaqueous medium as has been proved by others [2], we treated the complex of SPC1 with neat cyclohexane and then subjected it to X-ray diffraction analysis, and the result showed that all the 22 residues of SPC1 were located in the electron density map. So the topological structure of SPC1 has been determined, suggesting that crystal treatment with cyclohexane may be used as a method to determine the conformation of the disordered regions in protein crystal structures. X-Ray study on an artificial mung bean inhibitor complex with bovine beta-trypsin in neat cyclohexane.,Zhu G, Huang Q, Zhu Y, Li Y, Chi C, Tang Y Biochim Biophys Acta. 2001 Mar 9;1546(1):98-106. PMID:11257512[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||