1dos: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1dos.gif|left|200px]]


{{Structure
==STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE==
|PDB= 1dos |SIZE=350|CAPTION= <scene name='initialview01'>1dos</scene>, resolution 1.67&Aring;
<StructureSection load='1dos' size='340' side='right'caption='[[1dos]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NH4:AMMONIUM ION'>NH4</scene>
<table><tr><td colspan='2'>[[1dos]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DOS FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1dos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dos OCA], [https://pdbe.org/1dos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dos RCSB], [https://www.ebi.ac.uk/pdbsum/1dos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dos ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALF_ECOLI ALF_ECOLI] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.<ref>PMID:10712619</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dos_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1dos ConSurf].
<div style="clear:both"></div>


'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
==See Also==
 
*[[Aldolase 3D structures|Aldolase 3D structures]]
 
== References ==
==Overview==
<references/>
The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.
__TOC__
 
</StructureSection>
==About this Structure==
1DOS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOS OCA].
 
==Reference==
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase., Blom NS, Tetreault S, Coulombe R, Sygusch J, Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8836102 8836102]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Blom N]]
[[Category: Blom, N.]]
[[Category: Coulombe R]]
[[Category: Coulombe, R.]]
[[Category: Sygusch J]]
[[Category: Sygusch, J.]]
[[Category: Tetreault S]]
[[Category: Tetreault, S.]]
[[Category: NH4]]
[[Category: ZN]]
[[Category: 6-bisphosphate aldolase]]
[[Category: classii fructose 1]]
[[Category: glycolysis]]
[[Category: lyase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:54 2008''

Latest revision as of 06:57, 7 February 2024

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

1dos, resolution 1.67Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1dos&oldid=4042148"