3o08: Difference between revisions
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==Crystal structure of dimeric KlHxk1 in crystal form I== | ==Crystal structure of dimeric KlHxk1 in crystal form I== | ||
<StructureSection load='3o08' size='340' side='right' caption='[[3o08]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3o08' size='340' side='right'caption='[[3o08]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3o08]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3o08]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_56498 Atcc 56498]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O08 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o1b|3o1b]], [[3o1w|3o1w]], [[3o4w|3o4w]], [[3o5b|3o5b]], [[3o6w|3o6w]], [[3o8m|3o8m]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3o1b|3o1b]], [[3o1w|3o1w]], [[3o4w|3o4w]], [[3o5b|3o5b]], [[3o6w|3o6w]], [[3o8m|3o8m]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0D11352g, RAG5 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0D11352g, RAG5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28985 ATCC 56498])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hexokinase Hexokinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.1 2.7.1.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o08 OCA], [https://pdbe.org/3o08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o08 RCSB], [https://www.ebi.ac.uk/pdbsum/3o08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o08 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3o08" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3o08" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Hexokinase 3D structures|Hexokinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Atcc 56498]] | [[Category: Atcc 56498]] | ||
[[Category: Hexokinase]] | [[Category: Hexokinase]] | ||
[[Category: Large Structures]] | |||
[[Category: Keim, A]] | [[Category: Keim, A]] | ||
[[Category: Kettner, K]] | [[Category: Kettner, K]] | ||
Revision as of 10:12, 12 May 2022
Crystal structure of dimeric KlHxk1 in crystal form ICrystal structure of dimeric KlHxk1 in crystal form I
Structural highlights
Publication Abstract from PubMedCrystal structures of the unique hexokinase KlHxk1 of the yeast Kluyveromyces lactis were determined using eight independent crystal forms. In five crystal forms, a symmetrical ring-shaped homodimer was observed, corresponding to the physiological dimer existing in solution as shown by small-angle x-ray scattering. The dimer has a head-to-tail arrangement such that the small domain of one subunit interacts with the large domain of the other subunit. Dimer formation requires favorable interactions of the 15 N-terminal amino acids that are part of the large domain with amino acids of the small domain of the opposite subunit, respectively. The head-to-tail arrangement involving both domains of the two KlHxk1 subunits is appropriate to explain the reduced activity of the homodimer as compared with the monomeric enzyme and the influence of substrates and products on dimer formation and dissociation. In particular, the structure of the symmetrical KlHxk1 dimer serves to explain why phosphorylation of conserved residue Ser-15 may cause electrostatic repulsions with nearby negatively charged residues of the adjacent subunit, thereby inducing a dissociation of the homologous dimeric hexokinases KlHxk1 and ScHxk2. Two complex structures of KlHxk1 with bound glucose provide a molecular model of substrate binding to the open conformation and the subsequent classical domain closure motion of yeast hexokinases. The entirety of the novel data extends the current concept of glucose signaling in yeast and complements the induced-fit model by integrating the events of N-terminal phosphorylation and dissociation of homodimeric yeast hexokinases. Crystal Structure of Hexokinase KlHxk1 of Kluyveromyces lactis: A MOLECULAR BASIS FOR UNDERSTANDING THE CONTROL OF YEAST HEXOKINASE FUNCTIONS VIA COVALENT MODIFICATION AND OLIGOMERIZATION.,Kuettner EB, Kettner K, Keim A, Svergun DI, Volke D, Singer D, Hoffmann R, Muller EC, Otto A, Kriegel TM, Strater N J Biol Chem. 2010 Dec 24;285(52):41019-33. Epub 2010 Oct 12. PMID:20943665[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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