1l9m

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[[Image:1l9m.gif|left|200px]]<br /><applet load="1l9m" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l9m.gif|left|200px]]
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caption="1l9m, resolution 2.10&Aring;" />
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'''Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation'''<br />
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{{Structure
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|PDB= 1l9m |SIZE=350|CAPTION= <scene name='initialview01'>1l9m</scene>, resolution 2.10&Aring;
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|SITE=
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|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>
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|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]
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|GENE= TGM3 ([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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'''Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1L9M 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=BR:'>BR</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CA:'>CA</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=1L9M OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11980702 11980702]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:50 2008''
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''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


PDB ID 1l9m

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , and
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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