View source for 5ccf


==Structure of Mouse ADP-Dependent Glucokinase==
<StructureSection load='5ccf' size='340' side='right'caption='[[5ccf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ccf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCF 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]] 2.1&#8491;</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=5ccf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccf OCA], [https://pdbe.org/5ccf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccf RCSB], [https://www.ebi.ac.uk/pdbsum/5ccf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADPGK_MOUSE ADPGK_MOUSE] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme-catalyzed phosphorylation of glucose to glucose-6-phosphate is a reaction central to the metabolism of all life. ADP-dependent glucokinase (ADPGK) catalyzes glucose-6-phosphate production, utilizing ADP as a phosphoryl donor in contrast to the more well characterized ATP-requiring hexokinases. ADPGK is found in Archaea and metazoa; in Archaea, ADPGK participates in a glycolytic role, but a function in most eukaryotic cell types remains unknown. We have determined structures of the eukaryotic ADPGK revealing a ribokinase-like tertiary fold similar to archaeal orthologues but with significant differences in some secondary structural elements. Both the unliganded and the AMP-bound ADPGK structures are in the "open" conformation. The structures reveal the presence of a disulfide bond between conserved cysteines that is positioned at the nucleotide-binding loop of eukaryotic ADPGK. The AMP-bound ADPGK structure defines the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its main chain atoms, a nucleotide-binding motif that appears unique to eukaryotic ADPGKs. Key amino acids at the active site are structurally conserved between mammalian and archaeal ADPGK, and site-directed mutagenesis has confirmed residues essential for enzymatic activity. ADPGK is substrate inhibited by high glucose concentration and shows high specificity for glucose, with no activity for other sugars, as determined by NMR spectroscopy, including 2-deoxyglucose, the glucose analogue used for tumor detection by positron emission tomography.

The Structural and Functional Characterization of Mammalian ADP-dependent Glucokinase.,Richter JP, Goroncy AK, Ronimus RS, Sutherland-Smith AJ J Biol Chem. 2016 Feb 19;291(8):3694-704. doi: 10.1074/jbc.M115.679902. Epub 2015, Nov 10. PMID:26555263<ref>PMID:26555263</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ccf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Richter JP]]
[[Category: Ronimus RS]]
[[Category: Sutherland-Smith AJ]]