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.


1x9h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x9h.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1x9h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x9h| PDB=1x9h | SCENE= }}
{{STRUCTURE_1x9h| PDB=1x9h | SCENE= }}
-
'''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate'''
+
===Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate===
-
==Overview==
+
<!--
-
The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic sources, which cannot use M6P as a substrate, the equivalent residue is a glutamine. The increased space may permit rotation of the C2-C3 bond in M6P to facilitate abstraction of a proton from C2 by Glu203 and, after a further C2-C3 rotation of the resulting cis-enediolate, re-donation of a proton to C1 by the same residue. A proline residue (in place of a glycine in PGI) may also promote PMI activity by positioning the C1-O1 region of M6P. Thus, the PMI reaction in PaPGI/PMI probably uses a cis-enediol mechanism of catalysis, and this activity appears to arise from a subtle difference in the architecture of the enzyme, compared to bacterial and eukaryotic PGIs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15518558}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15518558 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15518558}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Hyperthermophile]]
[[Category: Hyperthermophile]]
[[Category: Pgi superfamily]]
[[Category: Pgi superfamily]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:44:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:02:40 2008''

Revision as of 12:02, 28 July 2008

Template:STRUCTURE 1x9h

Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate

Template:ABSTRACT PUBMED 15518558

About this Structure

1X9H is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.

Reference

Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes., Swan MK, Hansen T, Schonheit P, Davies C, Biochemistry. 2004 Nov 9;43(44):14088-95. PMID:15518558

Page seeded by OCA on Mon Jul 28 15:02:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools