View source for 4ast


==The apo structure of a bacterial aldo-keto reductase AKR14A1==
<StructureSection load='4ast' size='340' side='right'caption='[[4ast]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ast]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AST FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4aub|4aub]]</div></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=4ast FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ast OCA], [https://pdbe.org/4ast PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ast RCSB], [https://www.ebi.ac.uk/pdbsum/4ast PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ast ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/GPR_ECOLI GPR_ECOLI]] Catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.<ref>PMID:12583903</ref> <ref>PMID:16077126</ref> <ref>PMID:18620424</ref>  
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== Publication Abstract from PubMed ==
The genome of Escherichia coli K12 contains 9 open reading frames encoding aldo/keto reductases (AKRs) that are differentially regulated and sequence diverse. A significant amount of data is available for the E. coli AKRs through the availability of gene knockouts and gene expression studies, which adds to the biochemical and kinetic data. This together with the availability of crystal structures for nearly half of the E. coli AKRs and homologues of several others provides an opportunity to look at the diversity of these representative bacterial AKRs. Based around the common AKR fold of (beta/alpha)8 barrel with two additional alpha-helices, the E. coli AKRs have a loop structure that is more diverse than their mammalian counterparts, creating a variety of active site architectures. Nearly half of the AKRs are expected to be monomeric, but there are examples of dimeric, trimeric and octameric enzymes, as well as diversity in specificity for NAD as well as NADP as a cofactor. However in functional assignments and characterisation of enzyme activities there is a paucity of data when compared to the mammalian AKR enzymes.

The diversity of microbial aldo/keto reductases from Escherichia coli K12.,Lapthorn AJ, Zhu X, Ellis EM Chem Biol Interact. 2013 Feb 25;202(1-3):168-77. doi: 10.1016/j.cbi.2012.10.008. , Epub 2012 Oct 24. PMID:23103600<ref>PMID:23103600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ast" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Ellis, E M]]
[[Category: Lapthorn, A]]
[[Category: Zhu, X]]
[[Category: Oxidoreductase]]