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==Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G==
==Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G==
<StructureSection load='2f9o' size='340' side='right' caption='[[2f9o]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2f9o' size='340' side='right'caption='[[2f9o]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f9o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F9O FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F9O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</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=2f9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9o OCA], [https://pdbe.org/2f9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f9o RCSB], [https://www.ebi.ac.uk/pdbsum/2f9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9o ProSAT]</span></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f9n|2f9n]], [[2f9p|2f9p]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPSAB1, TPS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptase Tryptase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.59 3.4.21.59] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9o OCA], [http://pdbe.org/2f9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f9o RCSB], [http://www.ebi.ac.uk/pdbsum/2f9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9o ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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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=2f9o 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=2f9o ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tryptases alpha and beta are trypsin-like serine proteinases expressed in large amounts by mast cells. Beta-tryptase is a tetramer that has enzymatic activity, but requires heparin binding to maintain functional and structural stability, whereas alpha-tryptase has little, if any, enzymatic activity but is a stable tetramer in the absence of heparin. As shown previously, these differences can be mainly attributed to the different conformations of the 214-220 segment. Interestingly, the replacement of Asp216 by Gly, which is present in beta-tryptase, results in enzymatically active but less stable alpha-tryptase mutants. We have solved the crystal structures of both the single (D216G) and the double (K192Q/D216G) mutant forms of recombinant human alphaI-tryptase in complex with the peptide inhibitor leupeptin, as well as the structure of the non-inhibited single mutant. The inhibited mutants exhibited an open functional substrate binding site, while in the absence of an inhibitor, the open (beta-tryptase-like) and the closed (alpha-tryptase-like) conformations were present simultaneously. This shows that both forms are in a two-state equilibrium, which is influenced by the residues in the vicinity of the active site and by inhibitor/substrate binding. Novel insights regarding the observed stability differences as well as a potential proteolytic activity of wild-type alpha-tryptase, which may possess a cryptic active site, are discussed.
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha--&gt;beta-tryptase transition.,Rohr KB, Selwood T, Marquardt U, Huber R, Schechter NM, Bode W, Than ME J Mol Biol. 2006 Mar 17;357(1):195-209. Epub 2005 Dec 28. PMID:16414069<ref>PMID:16414069</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2f9o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tryptase|Tryptase]]
*[[Tryptase|Tryptase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Tryptase]]
[[Category: Bode W]]
[[Category: Bode, W]]
[[Category: Huber R]]
[[Category: Huber, R]]
[[Category: Marquardt U]]
[[Category: Marquardt, U]]
[[Category: Rohr KB]]
[[Category: Rohr, K B]]
[[Category: Schechter NM]]
[[Category: Schechter, N M]]
[[Category: Selwood T]]
[[Category: Selwood, T]]
[[Category: Than ME]]
[[Category: Than, M E]]
[[Category: Difucosylation]]
[[Category: Hydrolase]]
[[Category: Serine proteinase]]
[[Category: Trypsin-like]]
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