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.


1l6r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1l6r.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1l6r.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1l6r| PDB=1l6r | SCENE= }}
{{STRUCTURE_1l6r| PDB=1l6r | SCENE= }}
-
'''Crystal Structure of Thermoplasma acidophilum 0175 (APC0014)'''
+
===Crystal Structure of Thermoplasma acidophilum 0175 (APC0014)===
-
==Overview==
+
<!--
-
The protein TA0175 has a large number of sequence homologues, most of which are annotated as unknown and a few as belonging to the haloacid dehalogenase superfamily, but has no known biological function. Using a combination of amino acid sequence analysis, three-dimensional crystal structure information, and kinetic analysis, we have characterized TA0175 as phosphoglycolate phosphatase from Thermoplasma acidophilum. The crystal structure of TA0175 revealed two distinct domains, a larger core domain and a smaller cap domain. The large domain is composed of a centrally located five-stranded parallel beta-sheet with strand order S10, S9, S8, S1, S2 and a small beta-hairpin, strands S3 and S4. This central sheet is flanked by a set of three alpha-helices on one side and two helices on the other. The smaller domain is composed of an open faced beta-sandwich represented by three antiparallel beta-strands, S5, S6, and S7, flanked by two oppositely oriented alpha-helices, H3 and H4. The topology of the large domain is conserved; however, structural variation is observed in the smaller domain among the different functional classes of the haloacid dehalogenase superfamily. Enzymatic assays on TA0175 revealed that this enzyme catalyzed the dephosphorylation of phosphoglycolate in vitro with similar kinetic properties seen for eukaryotic phosphoglycolate phosphatase. Activation by divalent cations, especially Mg2+, and competitive inhibition behavior with Cl- ions are similar between TA0175 and phosphoglycolate phosphatase. The experimental evidence presented for TA0175 is indicative of phosphoglycolate phosphatase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14555659}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14555659 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14555659}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Putative hydrolase]]
[[Category: Putative hydrolase]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:36:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:49:36 2008''

Revision as of 08:49, 2 July 2008

Image:1l6r.png

Template:STRUCTURE 1l6r

Crystal Structure of Thermoplasma acidophilum 0175 (APC0014)

Template:ABSTRACT PUBMED 14555659

About this Structure

1L6R is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

Reference

Structure- and function-based characterization of a new phosphoglycolate phosphatase from Thermoplasma acidophilum., Kim Y, Yakunin AF, Kuznetsova E, Xu X, Pennycooke M, Gu J, Cheung F, Proudfoot M, Arrowsmith CH, Joachimiak A, Edwards AM, Christendat D, J Biol Chem. 2004 Jan 2;279(1):517-26. Epub 2003 Oct 10. PMID:14555659

Page seeded by OCA on Wed Jul 2 11:49:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l6r"
Personal tools