2bh9: Difference between revisions

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[[Image:2bh9.gif|left|200px]]<br /><applet load="2bh9" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2bh9.gif|left|200px]]
caption="2bh9, resolution 2.50&Aring;" />
 
'''X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP'''<br />
{{Structure
|PDB= 2bh9 |SIZE=350|CAPTION= <scene name='initialview01'>2bh9</scene>, resolution 2.50&Aring;
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]
|GENE=
}}
 
'''X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2BH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH9 OCA].  
2BH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH9 OCA].  


==Reference==
==Reference==
Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase., Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15858258 15858258]
Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase., Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15858258 15858258]
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: oxidoreductase (choh(d)-nadp)]]
[[Category: oxidoreductase (choh(d)-nadp)]]


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Revision as of 17:01, 20 March 2008

File:2bh9.gif


PDB ID 2bh9

Drag the structure with the mouse to rotate
, resolution 2.50Å
Sites:
Ligands: and
Activity: Glucose-6-phosphate 1-dehydrogenase, with EC number 1.1.1.49
Coordinates: save as pdb, mmCIF, xml



X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP


OverviewOverview

Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.

DiseaseDisease

Known diseases associated with this structure: Favism OMIM:[305900], G6PD deficiency OMIM:[305900], Hemolytic anemia due to G6PD deficiency OMIM:[305900]

About this StructureAbout this Structure

2BH9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase., Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258

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