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.


1wpp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wpp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1wpp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wpp| PDB=1wpp | SCENE= }}
{{STRUCTURE_1wpp| PDB=1wpp | SCENE= }}
-
'''Structure of Streptococcus gordonii inorganic pyrophosphatase'''
+
===Structure of Streptococcus gordonii inorganic pyrophosphatase===
-
==Overview==
+
<!--
-
Family II inorganic pyrophosphatases (PPases) constitute a new evolutionary group of PPases, with a different fold and mechanism than the common family I enzyme; they are related to the "DHH" family of phosphoesterases. Biochemical studies have shown that Mn(2+) and Co(2+) preferentially activate family II PPases; Mg(2+) partially activates; and Zn(2+) can either activate or inhibit (Zyryanov et al., Biochemistry, 43, 14395-14402, accompanying paper in this issue). The three solved family II PPase structures did not explain the differences between the PPase families nor the metal ion differences described above. We therefore solved three new family II PPase structures: Bacillus subtilis PPase (Bs-PPase) dimer core bound to Mn(2+) at 1.3 A resolution, and, at 2.05 A resolution, metal-free Bs-PPase and Streptococcus gordonii (Sg-PPase) containing sulfate and Zn(2+). Comparison of the new and old structures of various family II PPases demonstrates why the family II enzyme prefers Mn(2+) or Co(2+), as an activator rather than Mg(2+). Both M1 and M2 undergo significant changes upon substrate binding, changing from five-coordinate to octahedral geometry. Mn(2+) and Co(2+), which readily adopt different coordination states and geometries, are thus favored. Combining our structures with biochemical data, we identified M2 as the high-affinity metal site. Zn(2+) activates in the M1 site, where octahedral geometry is not essential for catalysis, but inhibits in the M2 site, because it is unable to assume octahedral geometry but remains trigonal bipyramidal. Finally, we propose that Lys205-Gln81-Gln80 form a hydrophilic channel to speed product release from the active site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15533045}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15533045 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15533045}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Inorganic pyrophosphatase]]
[[Category: Inorganic pyrophosphatase]]
[[Category: Metal binding]]
[[Category: Metal binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:59:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:57:37 2008''

Revision as of 14:57, 27 July 2008

Image:1wpp.png

Template:STRUCTURE 1wpp

Structure of Streptococcus gordonii inorganic pyrophosphatase

Template:ABSTRACT PUBMED 15533045

About this Structure

1WPP is a Single protein structure of sequence from Streptococcus gordonii str. challis. Full crystallographic information is available from OCA.

Reference

Structural studies of metal ions in family II pyrophosphatases: the requirement for a Janus ion., Fabrichniy IP, Lehtio L, Salminen A, Zyryanov AB, Baykov AA, Lahti R, Goldman A, Biochemistry. 2004 Nov 16;43(45):14403-11. PMID:15533045

Page seeded by OCA on Sun Jul 27 17:57:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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