3r1m: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Strucure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)== | |||
=== | <StructureSection load='3r1m' size='340' side='right' caption='[[3r1m]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3r1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_tokodaii Sulfolobus tokodaii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R1M FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1umg|1umg]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST0318 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=111955 Sulfolobus tokodaii])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r1m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r1m RCSB], [http://www.ebi.ac.uk/pdbsum/3r1m PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enzymes catalyse specific reactions and are essential for maintaining life. Although some are referred to as being bifunctional, they consist of either two distinct catalytic domains or a single domain that displays promiscuous substrate specificity. Thus, one enzyme active site is generally responsible for one biochemical reaction. In contrast to this conventional concept, archaeal fructose-1,6-bisphosphate (FBP) aldolase/phosphatase (FBPA/P) consists of a single catalytic domain, but catalyses two chemically distinct reactions of gluconeogenesis: (1) the reversible aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GA3P) to FBP; (2) the dephosphorylation of FBP to fructose-6-phosphate (F6P). Thus, FBPA/P is fundamentally different from ordinary enzymes whose active sites are responsible for a specific reaction. However, the molecular mechanism by which FBPA/P achieves its unusual bifunctionality remains unknown. Here we report the crystal structure of FBPA/P at 1.5-A resolution in the aldolase form, where a critical lysine residue forms a Schiff base with DHAP. A structural comparison of the aldolase form with a previously determined phosphatase form revealed a dramatic conformational change in the active site, demonstrating that FBPA/P metamorphoses its active-site architecture to exhibit dual activities. Thus, our findings expand the conventional concept that one enzyme catalyses one biochemical reaction. | |||
Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase.,Fushinobu S, Nishimasu H, Hattori D, Song HJ, Wakagi T Nature. 2011 Oct 9;478(7370):538-41. doi: 10.1038/nature10457. PMID:21983966<ref>PMID:21983966</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Suggestions for new articles|Suggestions for new articles]] | *[[Suggestions for new articles|Suggestions for new articles]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Sulfolobus tokodaii]] | [[Category: Sulfolobus tokodaii]] | ||
[[Category: Fushinobu, S | [[Category: Fushinobu, S]] | ||
[[Category: Hattori, D | [[Category: Hattori, D]] | ||
[[Category: Nishimasu, H | [[Category: Nishimasu, H]] | ||
[[Category: Song, H J | [[Category: Song, H J]] | ||
[[Category: Wakagi, T | [[Category: Wakagi, T]] | ||
[[Category: 6-bisphosphatase-like fold]] | [[Category: 6-bisphosphatase-like fold]] | ||
[[Category: Hydrolase/aldolase]] | [[Category: Hydrolase/aldolase]] | ||
Revision as of 08:37, 18 December 2014
Strucure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)
| ||||||||||||
