2dpn: Difference between revisions
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<StructureSection load='2dpn' size='340' side='right'caption='[[2dpn]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2dpn' size='340' side='right'caption='[[2dpn]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2dpn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DPN FirstGlance]. <br> | ||
</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=2dpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpn OCA], [https://pdbe.org/2dpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpn RCSB], [https://www.ebi.ac.uk/pdbsum/2dpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpn ProSAT], [https://www.topsan.org/Proteins/RSGI/2dpn TOPSAN]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=2dpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpn OCA], [https://pdbe.org/2dpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpn RCSB], [https://www.ebi.ac.uk/pdbsum/2dpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpn ProSAT], [https://www.topsan.org/Proteins/RSGI/2dpn TOPSAN]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q53W24_THET8 Q53W24_THET8] Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.[HAMAP-Rule:MF_00186] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus]] | ||
[[Category: | [[Category: Asada Y]] | ||
[[Category: | [[Category: Kunishima N]] | ||
[[Category: Sugahara | [[Category: Sugahara M]] | ||
Latest revision as of 11:28, 25 October 2023
Crystal Structure of the glycerol kinase from Thermus thermophilus HB8Crystal Structure of the glycerol kinase from Thermus thermophilus HB8
Structural highlights
FunctionQ53W24_THET8 Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.[HAMAP-Rule:MF_00186] 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 PubMedProtein crystallization is still a major bottleneck in structural biology. As the current methodology of protein crystallization is a type of screening, it is usually difficult to crystallize important target proteins. It was thought that hetero-epitaxic growth from the surface of a mineral crystal acting as a nucleant would be an effective enhancer of protein crystallization. However, in spite of almost two decades of effort, a generally applicable hetero-epitaxic nucleant for protein crystallization has yet to be found. Here we introduce the first candidate for a universal hetero-epitaxic nucleant, microporous zeolite: a synthetic aluminosilicate crystalline polymer with regular micropores. It promotes a form-selective crystal nucleation of proteins and acts as a crystallization catalyst. The most successful zeolite nucleant was molecular sieve type 5A with a pore size of 5 A and with bound Ca2+ ions. The zeolite-mediated crystallization improved the crystal quality in five out of six proteins tested. It provided new crystal forms with better resolution in two cases, larger crystals in one case, and zeolite-dependent crystal formations in two cases. The hetero-epitaxic growth of the zeolite-mediated crystals was confirmed by a crystal-packing analysis which revealed a layer-like structure in the crystal lattice. Nucleant-mediated protein crystallization with the application of microporous synthetic zeolites.,Sugahara M, Asada Y, Morikawa Y, Kageyama Y, Kunishima N Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):686-95. Epub 2008, May 14. PMID:18560157[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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