1tzc: Difference between revisions

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[[Image:1tzc.jpg|left|200px]]<br /><applet load="1tzc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1tzc.jpg|left|200px]]
caption="1tzc, resolution 1.45&Aring;" />
 
'''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate'''<br />
{{Structure
|PDB= 1tzc |SIZE=350|CAPTION= <scene name='initialview01'>1tzc</scene>, resolution 1.45&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PA5:5-PHOSPHOARABINONIC+ACID'>PA5</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY=
|GENE= PAE1610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=178306 Pyrobaculum aerophilum str. IM2])
}}
 
'''Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1TZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._im2 Pyrobaculum aerophilum str. im2] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PA5:'>PA5</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZC OCA].  
1TZC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._im2 Pyrobaculum aerophilum str. im2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZC OCA].  


==Reference==
==Reference==
A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution., Swan MK, Hansen T, Schonheit P, Davies C, J Biol Chem. 2004 Sep 17;279(38):39838-45. Epub 2004 Jul 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15252053 15252053]
A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution., Swan MK, Hansen T, Schonheit P, Davies C, J Biol Chem. 2004 Sep 17;279(38):39838-45. Epub 2004 Jul 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15252053 15252053]
[[Category: Pyrobaculum aerophilum str. im2]]
[[Category: Pyrobaculum aerophilum str. im2]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pgi family]]
[[Category: pgi family]]


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Revision as of 15:25, 20 March 2008

File:1tzc.jpg


PDB ID 1tzc

Drag the structure with the mouse to rotate
, resolution 1.45Å
Ligands: , and
Gene: PAE1610 (Pyrobaculum aerophilum str. IM2)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with 5-phosphoarabinonate


OverviewOverview

The crystal structure of a dual specificity phosphoglucose isomerase (PGI)/phosphomannose isomerase from Pyrobaculum aerophilum (PaPGI/PMI) has been determined in native form at 1.16-A resolution and in complex with the enzyme inhibitor 5-phosphoarabinonate at 1.45-A resolution. The similarity of its fold, with the inner core structure of PGIs from eubacterial and eukaryotic sources, confirms this enzyme as a member of the PGI superfamily. The almost total conservation of amino acids in the active site, including the glutamate base catalyst, shows that PaPGI/PMI uses the same catalytic mechanisms for both ring opening and isomerization for the interconversion of glucose 6-phosphate (Glc-6-P) to fructose 6-phosphate (Fru-6-P). The lack of structural differences between native and inhibitor-bound enzymes suggests this activity occurs without any of the conformational changes that are the hallmark of the well characterized PGI family. The lack of a suitable second base in the active site of PaPGI/PMI argues against a PMI mechanism involving a trans-enediol intermediate. Instead, PMI activity may be the result of additional space in the active site imparted by a threonine, in place of a glutamine in other PGI enzymes, which could permit rotation of the C-2-C-3 bond of mannose 6-phosphate.

About this StructureAbout this Structure

1TZC is a Single protein structure of sequence from Pyrobaculum aerophilum str. im2. Full crystallographic information is available from OCA.

ReferenceReference

A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution., Swan MK, Hansen T, Schonheit P, Davies C, J Biol Chem. 2004 Sep 17;279(38):39838-45. Epub 2004 Jul 13. PMID:15252053

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