1xsa
From Proteopedia
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[[Image:1xsa.gif|left|200px]] | [[Image:1xsa.gif|left|200px]] | ||
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'''Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)''' | '''Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)''' | ||
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==Reference== | ==Reference== | ||
Structure and substrate-binding mechanism of human Ap4A hydrolase., Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR, J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596429 15596429] | Structure and substrate-binding mechanism of human Ap4A hydrolase., Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR, J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596429 15596429] | ||
| - | [[Category: Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: McLennan, A G.]] | [[Category: McLennan, A G.]] | ||
[[Category: Swarbrick, J D.]] | [[Category: Swarbrick, J D.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta]] |
| - | [[Category: | + | [[Category: Human ap4a hydrolase]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Nudix enzyme]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:26:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:26, 3 May 2008
Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)
Overview
Asymmetric diadenosine 5',5-P(1),P(4)-tetraphosphate (Ap(4)A) hydrolases play a major role in maintaining homeostasis by cleaving the metabolite diadenosine tetraphosphate (Ap(4)A) back into ATP and AMP. The NMR solution structures of the 17-kDa human asymmetric Ap(4)A hydrolase have been solved in both the presence and absence of the product ATP. The adenine moiety of the nucleotide predominantly binds in a ring stacking arrangement equivalent to that observed in the x-ray structure of the homologue from Caenorhabditis elegans. The binding site is, however, markedly divergent to that observed in the plant/pathogenic bacteria class of enzymes, opening avenues for the exploration of specific therapeutics. Binding of ATP induces substantial conformational and dynamic changes that were not observed in the C. elegans structure. In contrast to the C. elegans homologue, important side chains that play a major role in substrate binding do not have to reorient to accommodate the ligand. This may have important implications in the mechanism of substrate recognition in this class of enzymes.
About this Structure
1XSA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and substrate-binding mechanism of human Ap4A hydrolase., Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR, J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. PMID:15596429 Page seeded by OCA on Sat May 3 15:26:57 2008
