2q3z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2q3z.jpg|left|200px]]<br /><applet load="2q3z" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2q3z.jpg|left|200px]]
-
caption="2q3z, resolution 2.000&Aring;" />
+
 
-
'''Transglutaminase 2 undergoes large conformational change upon activation'''<br />
+
{{Structure
 +
|PDB= 2q3z |SIZE=350|CAPTION= <scene name='initialview01'>2q3z</scene>, resolution 2.000&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13]
 +
|GENE= TGM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Transglutaminase 2 undergoes large conformational change upon activation'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2Q3Z 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=SO4:'>SO4</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-glutamine_gamma-glutamyltransferase Protein-glutamine gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.13 2.3.2.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3Z OCA].
+
2Q3Z 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=2Q3Z OCA].
==Reference==
==Reference==
-
Transglutaminase 2 undergoes a large conformational change upon activation., Pinkas DM, Strop P, Brunger AT, Khosla C, PLoS Biol. 2007 Dec;5(12):e327. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18092889 18092889]
+
Transglutaminase 2 undergoes a large conformational change upon activation., Pinkas DM, Strop P, Brunger AT, Khosla C, PLoS Biol. 2007 Dec;5(12):e327. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18092889 18092889]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
[[Category: Protein-glutamine gamma-glutamyltransferase]]
Line 26: Line 35:
[[Category: transglutaminase 2]]
[[Category: transglutaminase 2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:42 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:21:21 2008''

Revision as of 16:21, 20 March 2008


PDB ID 2q3z

Drag the structure with the mouse to rotate
, resolution 2.000Å
Ligands: , and
Gene: TGM2 (Homo sapiens)
Activity: Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13
Coordinates: save as pdb, mmCIF, xml



Transglutaminase 2 undergoes large conformational change upon activation


Overview

Human transglutaminase 2 (TG2), a member of a large family of enzymes that catalyze protein crosslinking, plays an important role in the extracellular matrix biology of many tissues and is implicated in the gluten-induced pathogenesis of celiac sprue. Although vertebrate transglutaminases have been studied extensively, thus far all structurally characterized members of this family have been crystallized in conformations with inaccessible active sites. We have trapped human TG2 in complex with an inhibitor that mimics inflammatory gluten peptide substrates and have solved, at 2-A resolution, its x-ray crystal structure. The inhibitor stabilizes TG2 in an extended conformation that is dramatically different from earlier transglutaminase structures. The active site is exposed, revealing that catalysis takes place in a tunnel, bridged by two tryptophan residues that separate acyl-donor from acyl-acceptor and stabilize the tetrahedral reaction intermediates. Site-directed mutagenesis was used to investigate the acyl-acceptor side of the tunnel, yielding mutants with a marked increase in preference for hydrolysis over transamidation. By providing the ability to visualize this activated conformer, our results create a foundation for understanding the catalytic as well as the non-catalytic roles of TG2 in biology, and for dissecting the process by which the autoantibody response to TG2 is induced in celiac sprue patients.

About this Structure

2Q3Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Transglutaminase 2 undergoes a large conformational change upon activation., Pinkas DM, Strop P, Brunger AT, Khosla C, PLoS Biol. 2007 Dec;5(12):e327. PMID:18092889

Page seeded by OCA on Thu Mar 20 18:21:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools