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.


2bh9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:38, 1 May 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2bh9.gif|left|200px]]<br /><applet load="2bh9" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
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 />
 
-
==Overview==
+
==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==
-
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.
+
<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2bh9]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [https://pdbe.org/2bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[https://omim.org/entry/305900 305900]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bh9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bh9 ConSurf].
 +
<div style="clear:both"></div>
-
==Disease==
+
==See Also==
-
Known diseases associated with this structure: Favism OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=305900 305900]], G6PD deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=305900 305900]], Hemolytic anemia due to G6PD deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=305900 305900]]
+
*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
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].
+
__TOC__
-
 
+
</StructureSection>
-
==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]
+
-
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Adams, M.J.]]
+
[[Category: Adams MJ]]
-
[[Category: Au, S.W.N.]]
+
[[Category: Au SWN]]
-
[[Category: Gover, S.]]
+
[[Category: Gover S]]
-
[[Category: Vandeputte-Rutten, L.]]
+
[[Category: Vandeputte-Rutten L]]
-
[[Category: GOL]]
+
-
[[Category: NAP]]
+
-
[[Category: carbohydrate metabolism]]
+
-
[[Category: glucose metabolism]]
+
-
[[Category: oxidoreductase (choh(d)-nadp)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:24:01 2008''
+

Current revision

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

PDB ID 2bh9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bh9"
Personal tools