2f9p

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[[Image:2f9p.gif|left|200px]]<br /><applet load="2f9p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2f9p.gif|left|200px]]
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caption="2f9p, resolution 2.30&Aring;" />
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'''Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin'''<br />
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{{Structure
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|PDB= 2f9p |SIZE=350|CAPTION= <scene name='initialview01'>2f9p</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>
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|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]
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|GENE= TPSAB1, TPS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2F9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=BU3:'>BU3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9P OCA].
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2F9P 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=2F9P OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16414069 16414069]
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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:[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:49:47 2008''

Revision as of 14:49, 20 March 2008

Image:2f9p.gif


PDB ID 2f9p

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , and
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 in Complex with Leupeptin


Overview

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 Structure

2F9P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

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:16414069

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