1kv3
From Proteopedia
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| - | [[Image:1kv3.gif|left|200px]] | + | [[Image:1kv3.gif|left|200px]] |
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| - | '''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM''' | + | {{Structure |
| + | |PDB= 1kv3 |SIZE=350|CAPTION= <scene name='initialview01'>1kv3</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</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]) | ||
| + | }} | ||
| + | |||
| + | '''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KV3 is a [ | + | 1KV3 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=1KV3 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity., Liu S, Cerione RA, Clardy J, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. Epub 2002 Feb 26. PMID:[http:// | + | Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity., Liu S, Cerione RA, Clardy J, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. Epub 2002 Feb 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11867708 11867708] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
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[[Category: tissue transglutaminase; gtp binding protein; crystallography]] | [[Category: tissue transglutaminase; gtp binding protein; crystallography]] | ||
| - | ''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 12:22:29 2008'' |
Revision as of 10:22, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Gene: | TGM2 (Homo sapiens) | ||||||
| Activity: | Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM
Overview
Tissue transglutaminase (TG) is a Ca2+-dependent acyltransferase with roles in cellular differentiation, apoptosis, and other biological functions. In addition to being a transamidase, TG undergoes a GTP-binding/GTPase cycle even though it lacks any obvious sequence similarity with canonical GTP-binding (G) proteins. Guanine nucleotide binding and Ca2+ concentration reciprocally regulate TG's transamidation activity, with nucleotide binding being the negative regulator. Here we report the x-ray structure determined to 2.8-A resolution of human TG complexed with GDP. Although the transamidation active site is similar to those of other known transglutaminases, the guanine nucleotide-binding site of TG differs markedly from other G proteins. The structure suggests a structural basis for the negative regulation of transamidation activity by bound nucleotide, and the positive regulation of transamidation by Ca2+.
About this Structure
1KV3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity., Liu S, Cerione RA, Clardy J, Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2743-7. Epub 2002 Feb 26. PMID:11867708
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