1l9m: Difference between revisions
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[[Image:1l9m.gif|left|200px]] | [[Image:1l9m.gif|left|200px]] | ||
'''Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation''' | {{Structure | ||
|PDB= 1l9m |SIZE=350|CAPTION= <scene name='initialview01'>1l9m</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</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= TGM3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L9M is a [ | 1L9M 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=1L9M OCA]. | ||
==Reference== | ==Reference== | ||
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation., Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM, EMBO J. 2002 May 1;21(9):2055-67. PMID:[http:// | Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation., Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM, EMBO J. 2002 May 1;21(9):2055-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11980702 11980702] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
''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 12:28:16 2008'' | ||
Revision as of 10:28, 20 March 2008
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| 1l9m, resolution 2.10Å | |||||||||||||
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| Ligands: | BR, CL and CA | ||||||||||||
| Gene: | TGM3 (Homo sapiens) | ||||||||||||
| Activity: | Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
Overview
Transglutaminase (TGase) enzymes catalyze the formation of covalent cross-links between protein-bound glutamines and lysines in a calcium-dependent manner, but the role of Ca(2+) ions remains unclear. The TGase 3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. We have solved the three-dimensional structures of the zymogen and the activated forms at 2.2 and 2.1 A resolution, respectively, and examined the role of Ca(2+) ions. The zymogen binds one ion tightly that cannot be exchanged. Upon proteolysis, the enzyme exothermally acquires two more Ca(2+) ions that activate the enzyme, are exchangeable and are functionally replaceable by other lanthanide trivalent cations. Binding of a Ca(2+) ion at one of these sites opens a channel which exposes the key Trp236 and Trp327 residues that control substrate access to the active site. Together, these biochemical and structural data reveal for the first time in a TGase enzyme that Ca(2+) ions induce structural changes which at least in part dictate activity and, moreover, may confer substrate specificity.
About this Structure
1L9M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation., Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM, EMBO J. 2002 May 1;21(9):2055-67. PMID:11980702
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