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1kv3
From Proteopedia
(New page: 200px<br /> <applet load="1kv3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kv3, resolution 2.80Å" /> '''HUMAN TISSUE TRANSG...) |
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| - | [[Image:1kv3.gif|left|200px]]<br /> | + | [[Image:1kv3.gif|left|200px]]<br /><applet load="1kv3" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1kv3" size=" | + | |
caption="1kv3, resolution 2.80Å" /> | caption="1kv3, resolution 2.80Å" /> | ||
'''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM'''<br /> | '''HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tissue transglutaminase (TG) is a Ca2+-dependent acyltransferase with | + | 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== | ==About this Structure== | ||
| - | 1KV3 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 GDP as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1KV3 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=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1KV3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-glutamine gamma-glutamyltransferase]] | [[Category: Protein-glutamine gamma-glutamyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cerione, R | + | [[Category: Cerione, R A.]] |
[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
[[Category: Liu, S.]] | [[Category: Liu, S.]] | ||
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[[Category: tissue transglutaminase; gtp binding protein; crystallography]] | [[Category: tissue transglutaminase; gtp binding protein; crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:11 2008'' |
Revision as of 11:38, 21 February 2008
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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 with as ligand. Active as Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 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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