1dea: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1dea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dea, resolution 2.1Å" /> '''STRUCTURE AND CATALYT...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1dea.jpg|left|200px]]<br /><applet load="1dea" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dea, resolution 2.1&Aring;" />
'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''<br />


==Overview==
==STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION==
BACKGROUND: Glucosamine 6-phosphate deaminase from Escherichia coli is an, allosteric hexameric enzyme which catalyzes the reversible conversion of, D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and, is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it, belongs to the group of aldoseketose isomerases, but its reaction also, accomplishes a simultaneous amination/deamination. The determination of, the structure of this protein provides fundamental knowledge for, understanding its mode of action and the nature of allosteric, conformational changes that regulate its function. RESULTS: The crystal, structure of glucosamine 6-phosphate deaminase with bound phosphate ions, is presented at 2.1 A resolution together with the refined structures of, the enzyme in complexes with its allosteric activator and with a, competitive inhibitor. The protein fold can be described as a modified, NAD-binding domain. CONCLUSIONS: From the similarities between the three, presented structures, it is concluded that these represent the, enzymatically active R state conformer. A mechanism for the deaminase, reaction is proposed. It comprises steps to open the pyranose ring of the, substrate and a sequence of general base-catalyzed reactions to bring, about isomerization and deamination, with Asp72 playing a key role as a, proton exchanger.
<StructureSection load='1dea' size='340' side='right'caption='[[1dea]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dea]] 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=1DEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1dea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dea OCA], [https://pdbe.org/1dea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dea RCSB], [https://www.ebi.ac.uk/pdbsum/1dea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAGB_ECOLI NAGB_ECOLI] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.[HAMAP-Rule:MF_01241]
== 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/de/1dea_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=1dea ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEA OCA].
*[[Deaminase 3D structures|Deaminase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution., Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E, Structure. 1995 Dec 15;3(12):1323-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8747459 8747459]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glucosamine-6-phosphate deaminase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Altamirano MM]]
[[Category: Altamirano, M.M.]]
[[Category: Calcagno ML]]
[[Category: Calcagno, M.L.]]
[[Category: Fontes MRM]]
[[Category: Fontes, M.R.M.]]
[[Category: Garratt RC]]
[[Category: Garratt, R.C.]]
[[Category: Horjales E]]
[[Category: Horjales, E.]]
[[Category: Oliva G]]
[[Category: Oliva, G.]]
[[Category: PO4]]
[[Category: intramolecular oxidoreductase deaminase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:12:51 2007''

Latest revision as of 06:52, 7 February 2024

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

1dea, resolution 2.10Å

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=1dea&oldid=4041829"