1ub3

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[[Image:1ub3.jpg|left|200px]]<br /><applet load="1ub3" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ub3, resolution 1.40&Aring;" />
 
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'''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''<br />
 
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==Overview==
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==Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8==
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<StructureSection load='1ub3' size='340' side='right'caption='[[1ub3]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ub3]] is a 4 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=1UB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UB3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HPD:1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE'>HPD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ub3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ub3 OCA], [https://pdbe.org/1ub3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ub3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ub3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ub3 ProSAT], [https://www.topsan.org/Proteins/RSGI/1ub3 TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEOC_THET8 DEOC_THET8] Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate (By similarity).[HAMAP-Rule:MF_00114]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ub/1ub3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ub3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol condensation of two aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue. The crystal structure of 2-deoxyribose-5-phosphate aldolase from Thermus thermophilus HB8 has been determined with and without the substrate at atomic resolution. This enzyme, which has a unique homotetramer structure, has been compared with the previously reported crystal structures of two orthologues from Escherichia coli and Aeropyrum pernix. In contrast to the similar alpha/beta-barrel fold of the monomers, substantial quaternary structural differences are observed between these three enzymes. Further comparison of the subunit-subunit interface areas of these aldolases showed a clear positive correlation between the interface area and the living temperature of the source organism. From these results, it is concluded that the oligomeric state of 2-deoxyribose-5-phosphate aldolase is important for the thermostability and not for the catalytic function.
2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol condensation of two aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue. The crystal structure of 2-deoxyribose-5-phosphate aldolase from Thermus thermophilus HB8 has been determined with and without the substrate at atomic resolution. This enzyme, which has a unique homotetramer structure, has been compared with the previously reported crystal structures of two orthologues from Escherichia coli and Aeropyrum pernix. In contrast to the similar alpha/beta-barrel fold of the monomers, substantial quaternary structural differences are observed between these three enzymes. Further comparison of the subunit-subunit interface areas of these aldolases showed a clear positive correlation between the interface area and the living temperature of the source organism. From these results, it is concluded that the oligomeric state of 2-deoxyribose-5-phosphate aldolase is important for the thermostability and not for the catalytic function.
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==About this Structure==
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Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.,Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1816-23. Epub 2004, Sep 23. PMID:15388928<ref>PMID:15388928</ref>
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1UB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=HPD:'>HPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability., Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1816-23. Epub 2004, Sep 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15388928 15388928]
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</div>
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[[Category: Deoxyribose-phosphate aldolase]]
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<div class="pdbe-citations 1ub3" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Kunishima, N.]]
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[[Category: Kuramitsu, S.]]
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[[Category: Lokanath, N K.]]
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[[Category: Miyano, M.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Yokoyama, S.]]
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[[Category: HPD]]
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[[Category: carbinolamine]]
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[[Category: deoxyribose phosphate]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: schiff base]]
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[[Category: structural genomics]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:29 2008''
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==See Also==
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*[[Aldolase 3D structures|Aldolase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus]]
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[[Category: Kunishima N]]
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[[Category: Kuramitsu S]]
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[[Category: Lokanath NK]]
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[[Category: Miyano M]]
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[[Category: Yokoyama S]]

Current revision

Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8

PDB ID 1ub3

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