2q3z
From Proteopedia
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|PDB= 2q3z |SIZE=350|CAPTION= <scene name='initialview01'>2q3z</scene>, resolution 2.000Å | |PDB= 2q3z |SIZE=350|CAPTION= <scene name='initialview01'>2q3z</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ONL:5-OXO-L-NORLEUCINE'>ONL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= TGM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= TGM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1kv3|1kv3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3z OCA], [http://www.ebi.ac.uk/pdbsum/2q3z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q3z RCSB]</span> | ||
}} | }} | ||
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[[Category: Pinkas, D M.]] | [[Category: Pinkas, D M.]] | ||
[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
| - | [[Category: SO4]] | ||
[[Category: tg2]] | [[Category: tg2]] | ||
[[Category: tissue transglutaminase]] | [[Category: tissue transglutaminase]] | ||
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[[Category: transglutaminase 2]] | [[Category: transglutaminase 2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:44:20 2008'' |
Revision as of 01:44, 31 March 2008
| |||||||
| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | TGM2 (Homo sapiens) | ||||||
| Activity: | Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 | ||||||
| Related: | 1kv3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 04:44:20 2008
