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2j8t

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Revision as of 06:47, 11 July 2018

Human aldose reductase in complex with NADP and citrate at 0.82 angstrom

Structural highlights

2j8t is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2fzb, 2fzd
Activity:	Aldehyde reductase, with EC number 1.1.1.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of human aldose reductase in complex with citrate has been determined to a resolution of 0.82 A. The difference electron density for H atoms unequivocally shows that the cofactor is in the oxidized state corresponding to the situation after the catalytic event has occurred. A citrate molecule bound to the active site has been modelled in two different conformations. These two conformations correlate with a fully closed and a partially open conformation of the so-called safety-belt loop (Gly213-Ser226). The open conformation is observed for the first time with the cofactor bound to the protein and may be related to the initial phase of the opening of the safety belt. The structure suggests that after the catalytic event, a rearrangement of a bound ligand can trigger the opening of the safety-belt loop, thus initiating the release of the oxidized cofactor.

The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.,Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007, May 15. PMID:17505104^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR. The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007, May 15. PMID:17505104 doi:10.1107/S0907444907011997

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j8t"

@@ Line 1: / Line 1: @@
-==HUMAN ALDOSE REDUCTASE IN COMPLEX WITH NADP AND CITRATE AT 0.82 ANGSTROM==
+==Human aldose reductase in complex with NADP and citrate at 0.82 angstrom==
 <StructureSection load='2j8t' size='340' side='right' caption='[[2j8t]], [[Resolution|resolution]] 0.82&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fzb|2fzb]], [[2fzd|2fzd]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8t OCA], [http://pdbe.org/2j8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j8t RCSB], [http://www.ebi.ac.uk/pdbsum/2j8t PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8t OCA], [http://pdbe.org/2j8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j8t RCSB], [http://www.ebi.ac.uk/pdbsum/2j8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8t ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j8/2j8t_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j8/2j8t_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 32: @@
 ==See Also==
-*[[Aldose Reductase|Aldose Reductase]]
+*[[Aldo-keto reductase|Aldo-keto reductase]]
 == References ==
 <references/>

2j8t

From Proteopedia

Revision as of 06:47, 11 July 2018

Human aldose reductase in complex with NADP and citrate at 0.82 angstrom

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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