1xsa: Difference between revisions

Revision as of 07:53, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xsa.png

Template:STRUCTURE 1xsa

Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant)

Template:ABSTRACT PUBMED 15596429

About this StructureAbout this Structure

1XSA is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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)===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15596429}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15596429 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15596429}}
 ==About this Structure==
-XSA 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=1XSA OCA].
+XSA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSA OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Nudix enzyme]]
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