2bkv: Difference between revisions

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New page: left|200px<br /> <applet load="2bkv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bkv, resolution 1.504Å" /> '''STRUCTURE AND KINE...
 
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[[Image:2bkv.gif|left|200px]]<br />
<applet load="2bkv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bkv, resolution 1.504&Aring;" />
'''STRUCTURE AND KINETICS OF A MONOMERIC GLUCOSAMINE-6-PHOSPHATE DEAMINASE: MISSING LINK OF THE NAGB SUPERFAMILY'''<br />


==Overview==
==Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the NagB superfamily==
Glucosamine 6-phosphate is converted to fructose 6-phosphate and ammonia, by the action of the enzyme glucosamine 6-phosphate deaminase, NagB. This, reaction is the final step in the specific GlcNAc utilization pathway and, thus decides the metabolic fate of GlcNAc. Sequence analyses suggest that, the NagB "superfamily" consists of three main clusters: multimeric and, allosterically regulated glucosamine-6-phosphate deaminases (exemplified, by Escherichia coli NagB), phosphogluconolactonases, and monomeric, hexosamine-6-phosphate deaminases. Here we present the three-dimensional, structure and kinetics of the first member of this latter group, the, glucosamine-6-phosphate deaminase, NagB, from Bacillus subtilis. The, structures were determined in ligand-complexed forms at resolutions ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15755726 (full description)]]
<StructureSection load='2bkv' size='340' side='right'caption='[[2bkv]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bkv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BKV 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</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=2bkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bkv OCA], [https://pdbe.org/2bkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bkv RCSB], [https://www.ebi.ac.uk/pdbsum/2bkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bkv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAGB_BACSU NAGB_BACSU] Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion (By similarity).
== 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/bk/2bkv_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=2bkv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2BKV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]] with PGA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=2BKV OCA]].
*[[Deaminase 3D structures|Deaminase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily?, Vincent F, Davies GJ, Brannigan JA, J Biol Chem. 2005 May 20;280(20):19649-55. Epub 2005 Mar 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15755726 15755726]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brannigan, J.A.]]
[[Category: Brannigan JA]]
[[Category: Davies, G.J.]]
[[Category: Davies GJ]]
[[Category: Vincent, F.]]
[[Category: Vincent F]]
[[Category: PGA]]
[[Category: fructose-6-phosphate]]
[[Category: hydrolase]]
[[Category: substrate inhibition]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:33:59 2007''

Latest revision as of 09:38, 1 May 2024

Structure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the NagB superfamilyStructure and kinetics of a monomeric glucosamine-6-phosphate deaminase: missing link of the NagB superfamily

Structural highlights

2bkv is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NAGB_BACSU Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2bkv, resolution 1.50Å

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