This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1xsb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xsb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xsb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xsb| PDB=1xsb | SCENE= }}
{{STRUCTURE_1xsb| PDB=1xsb | SCENE= }}
-
'''Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP. No ATP restraints included'''
+
===Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP. No ATP restraints included===
-
==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==
==About this Structure==
-
1XSB 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=1XSB OCA].
+
1XSB 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=1XSB OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Nudix enzyme]]
[[Category: Nudix enzyme]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:27:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:47:32 2008''

Revision as of 07:47, 29 July 2008

Image:1xsb.png

Template:STRUCTURE 1xsb

Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP. No ATP restraints included

Template:ABSTRACT PUBMED 15596429

About this Structure

1XSB is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Tue Jul 29 10:47:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xsb"
Personal tools