2f9o: Difference between revisions
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[[Image:2f9o.gif|left|200px]] | [[Image:2f9o.gif|left|200px]] | ||
'''Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G''' | {{Structure | ||
|PDB= 2f9o |SIZE=350|CAPTION= <scene name='initialview01'>2f9o</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= TPSAB1, TPS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2F9O is a [ | 2F9O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9O OCA]. | ||
==Reference== | ==Reference== | ||
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->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:[http:// | X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->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:[http://www.ncbi.nlm.nih.gov/pubmed/16414069 16414069] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trypsin-like]] | [[Category: trypsin-like]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:49:50 2008'' | ||
Revision as of 17:49, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Gene: | TPSAB1, TPS1 (Homo sapiens) | ||||||
| Activity: | Tryptase, with EC number 3.4.21.59 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G
OverviewOverview
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.
About this StructureAbout this Structure
2F9O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->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
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