1j2w: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1j2w' size='340' side='right'caption='[[1j2w]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1j2w' size='340' side='right'caption='[[1j2w]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j2w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j2w]] 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=1J2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2W 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=1j2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2w OCA], [https://pdbe.org/1j2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2w RCSB], [https://www.ebi.ac.uk/pdbsum/1j2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2w ProSAT], [https://www.topsan.org/Proteins/RSGI/1j2w 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]] 1.5Å</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=1j2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2w OCA], [https://pdbe.org/1j2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2w RCSB], [https://www.ebi.ac.uk/pdbsum/1j2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2w ProSAT], [https://www.topsan.org/Proteins/RSGI/1j2w TOPSAN]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[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] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 34: | Line 35: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kunishima | [[Category: Thermus thermophilus]] | ||
[[Category: Kuramitsu | [[Category: Kunishima N]] | ||
[[Category: Lokanath | [[Category: Kuramitsu S]] | ||
[[Category: Miyano | [[Category: Lokanath NK]] | ||
[[Category: Miyano M]] | |||
[[Category: Shiromizu | [[Category: Shiromizu I]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 02:41, 28 December 2023
Tetrameric Structure of aldolase from Thermus thermophilus HB8Tetrameric Structure of aldolase from Thermus thermophilus HB8
Structural highlights
FunctionDEOC_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] 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 PubMed2-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||