We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2j6h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_2j6h| PDB=2j6h | SCENE= }}
+
==E. COLI GLUCOSAMINE-6-P SYNTHASE IN COMPLEX WITH GLUCOSE-6P AND 5-OXO-L-NORLEUCINE==
-
===E. COLI GLUCOSAMINE-6-P SYNTHASE IN COMPLEX WITH GLUCOSE-6P AND 5-OXO-L-NORLEUCINE===
+
<StructureSection load='2j6h' size='340' side='right' caption='[[2j6h]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_16339762}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2j6h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bpj 2bpj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J6H FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>, <scene name='pdbligand=ONL:5-OXO-L-NORLEUCINE'>ONL</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jxa|1jxa]], [[1moq|1moq]], [[1mor|1mor]], [[1mos|1mos]], [[1xff|1xff]], [[1xfg|1xfg]], [[2bpl|2bpl]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j6h RCSB], [http://www.ebi.ac.uk/pdbsum/2j6h PDBsum]</span></td></tr>
 +
<table>
 +
== 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/j6/2j6h_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine and uses a channel to transfer ammonia from its glutaminase to its synthase active site. X-ray structures of glucosamine-6P synthase have been determined at 2.05 Angstroms resolution in the presence of fructose-6P and at 2.35 Angstroms resolution in the presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine affinity analog that covalently modifies the N-terminal catalytic cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate formed during hydrolysis of glutamine. The fixation of the glutamine analog activates the enzyme through several major structural changes: 1) the closure of a loop to shield the glutaminase site accompanied by significant domain hinging, 2) the activation of catalytic residues involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees rotation of the Trp-74 indole group that opens the ammonia channel.
-
==Function==
+
Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase.,Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:16339762<ref>PMID:16339762</ref>
-
[[http://www.uniprot.org/uniprot/GLMS_ECOLI GLMS_ECOLI]] Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[2j6h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bpj 2bpj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6H OCA].
+
</div>
==See Also==
==See Also==
*[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]]
*[[Glucosamine 6-phosphate synthase|Glucosamine 6-phosphate synthase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:016339762</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Golinelli-Pimpaneau, B.]]
[[Category: Golinelli-Pimpaneau, B.]]

Revision as of 04:17, 3 October 2014

E. COLI GLUCOSAMINE-6-P SYNTHASE IN COMPLEX WITH GLUCOSE-6P AND 5-OXO-L-NORLEUCINE

2j6h, resolution 2.35Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j6h"
Views
Personal tools
Navigation
Toolbox