1x9i: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1x9i.jpg|left|200px]]
{{Seed}}
[[Image:1x9i.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x9i|  PDB=1x9i  |  SCENE=  }}  
{{STRUCTURE_1x9i|  PDB=1x9i  |  SCENE=  }}  


'''Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate'''
===Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 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 Sun Jul 27 19:18:43 2008''

Revision as of 16:18, 27 July 2008

File:1x9i.png

Template:STRUCTURE 1x9i

Crystal structure of Crystal structure of phosphoglucose/phosphomannose phosphoglucose/phosphomannoseisomerase from Pyrobaculum aerophilum in complex with glucose 6-phosphate

Template:ABSTRACT PUBMED 15518558

About this Structure

1X9I 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 Sun Jul 27 19:18:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1x9i&oldid=662744"