3beu: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (18 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity== | ||
<StructureSection load='3beu' size='340' side='right'caption='[[3beu]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
[ | <table><tr><td colspan='2'>[[3beu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BEU 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]] 1.05Å</td></tr> | ||
[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=3beu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3beu OCA], [https://pdbe.org/3beu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3beu RCSB], [https://www.ebi.ac.uk/pdbsum/3beu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3beu ProSAT]</span></td></tr> | ||
[[ | </table> | ||
[ | == Function == | ||
[[ | [https://www.uniprot.org/uniprot/TRYP_STRGR TRYP_STRGR] | ||
[ | == 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/be/3beu_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=3beu ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Some trypsin-like proteases are endowed with Na(+)-dependent allosteric enhancement of catalytic activity, but this important mechanism has been difficult to engineer in other members of the family. Replacement of 19 amino acids in Streptomyces griseus trypsin targeting the active site and the Na(+)-binding site were found necessary to generate efficient Na(+) activation. Remarkably, this property was linked to the acquisition of a new substrate selectivity profile similar to that of factor Xa, a Na(+)-activated protease involved in blood coagulation. The X-ray crystal structure of the mutant trypsin solved to 1.05 A resolution defines the engineered Na(+) site and active site loops in unprecedented detail. The results demonstrate that trypsin can be engineered into an efficient allosteric protease, and that Na(+) activation is interwoven with substrate selectivity in the trypsin scaffold. | |||
Engineering protein allostery: 1.05 A resolution structure and enzymatic properties of a Na+-activated trypsin.,Page MJ, Carrell CJ, Di Cera E J Mol Biol. 2008 May 2;378(3):666-72. Epub 2008 Mar 18. PMID:18377928<ref>PMID:18377928</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3beu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin 3D structures|Trypsin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces griseus]] | |||
[[Category: Carrell CJ]] | |||
[[Category: Di Cera E]] | |||
[[Category: Page MJ]] | |||
Latest revision as of 08:42, 17 October 2024
Na+-Dependent Allostery Mediates Coagulation Factor Protease Active Site SelectivityNa+-Dependent Allostery Mediates Coagulation Factor Protease Active Site Selectivity
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 PubMedSome trypsin-like proteases are endowed with Na(+)-dependent allosteric enhancement of catalytic activity, but this important mechanism has been difficult to engineer in other members of the family. Replacement of 19 amino acids in Streptomyces griseus trypsin targeting the active site and the Na(+)-binding site were found necessary to generate efficient Na(+) activation. Remarkably, this property was linked to the acquisition of a new substrate selectivity profile similar to that of factor Xa, a Na(+)-activated protease involved in blood coagulation. The X-ray crystal structure of the mutant trypsin solved to 1.05 A resolution defines the engineered Na(+) site and active site loops in unprecedented detail. The results demonstrate that trypsin can be engineered into an efficient allosteric protease, and that Na(+) activation is interwoven with substrate selectivity in the trypsin scaffold. Engineering protein allostery: 1.05 A resolution structure and enzymatic properties of a Na+-activated trypsin.,Page MJ, Carrell CJ, Di Cera E J Mol Biol. 2008 May 2;378(3):666-72. Epub 2008 Mar 18. PMID:18377928[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||