1cnq

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[[Image:1cnq.jpg|left|200px]]<br /><applet load="1cnq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cnq.jpg|left|200px]]
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caption="1cnq, resolution 2.27&Aring;" />
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'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE AND ZINC IONS'''<br />
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{{Structure
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|PDB= 1cnq |SIZE=350|CAPTION= <scene name='initialview01'>1cnq</scene>, resolution 2.27&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11]
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|GENE=
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}}
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'''FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE AND ZINC IONS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1CNQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=F6P:'>F6P</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1BFL. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNQ OCA].
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1CNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry 1BFL. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNQ OCA].
==Reference==
==Reference==
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Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase., Choe JY, Poland BW, Fromm HJ, Honzatko RB, Biochemistry. 1998 Aug 18;37(33):11441-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9708979 9708979]
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Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase., Choe JY, Poland BW, Fromm HJ, Honzatko RB, Biochemistry. 1998 Aug 18;37(33):11441-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9708979 9708979]
[[Category: Fructose-bisphosphatase]]
[[Category: Fructose-bisphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:38 2008''

Revision as of 08:26, 20 March 2008

Image:1cnq.jpg


PDB ID 1cnq

Drag the structure with the mouse to rotate
, resolution 2.27Å
Ligands: , and
Activity: Fructose-bisphosphatase, with EC number 3.1.3.11
Coordinates: save as pdb, mmCIF, xml



FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-6-PHOSPHATE AND ZINC IONS


Overview

A disordered loop (loop 52-72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated in regulatory and catalytic phenomena by studies in directed mutation. A crystal structure of FBPase in a complex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals loop 52-72 for the first time in a well-defined conformation with strong electron density. Loop 52-57 interacts primarily with the active site of its own subunit. Asp68 of the loop hydrogen bonds with Arg276 and a zinc cation located at the putative potassium activation site. Leu56 and Tyr57 of the loop pack against hydrophobic residues from two separate subunits of FBPase. A mechanism of allosteric regulation of catalysis is presented, in which AMP, by binding to its allosteric pocket, displaces loop 52-72 from the active site. Furthermore, the current structure suggests that both the alpha- and beta-anomers of F6P can be substrates in the reverse reaction catalyzed by FBPase. Mechanisms of catalysis are proposed for the reverse reaction in which Asp121 serves as a catalytic base for the alpha-anomer and Glu280 serves as a catalytic base for the beta-anomer.

About this Structure

1CNQ is a Single protein structure of sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1BFL. Full crystallographic information is available from OCA.

Reference

Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase., Choe JY, Poland BW, Fromm HJ, Honzatko RB, Biochemistry. 1998 Aug 18;37(33):11441-50. PMID:9708979

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