2d33: 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
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2d33.png|left|200px]]


<!--
==Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride==
The line below this paragraph, containing "STRUCTURE_2d33", creates the "Structure Box" on the page.
<StructureSection load='2d33' size='340' side='right'caption='[[2d33]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2d33]] is a 4 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=2D33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D33 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_2d33|  PDB=2d33  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d33 OCA], [https://pdbe.org/2d33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d33 RCSB], [https://www.ebi.ac.uk/pdbsum/2d33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d33 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSH1_ECOLI GSH1_ECOLI]
== 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/d3/2d33_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2d33 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Escherichia coli B gamma-glutamylcysteine synthetase (gammaGCS) catalyzes the ATP-dependent coupling of L-Glu and L-Cys to form the glutathione precursor gamma-L-Glu-Cys and is a target for development of potential therapeutic agents. By introducing four point mutations of surface-exposed cysteine residues to serine, the gammaGCS was purified to homogeneity; single crystals have been obtained using the hanging-drop vapour-diffusion method with sodium formate. The gammaGCS crystal diffracted to 2.8 A and belongs to space group R3, with unit-cell parameters a = b = 326.7, c = 103.9 A.


===Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride===
Escherichia coli B gamma-glutamylcysteine synthetase: modification, purification, crystallization and preliminary crystallographic analysis.,Hibi T, Hisada H, Nakatsu T, Kato H, Oda J Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):316-8. Epub 2002, Jan 24. PMID:011807262<ref>PMID:011807262</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
2D33 is a 4 chains structure of sequences 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=2D33 OCA].
<div class="pdbe-citations 2d33" style="background-color:#fffaf0;"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:15477603</ref><ref group="xtra">PMID:11807262</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamate--cysteine ligase]]
[[Category: Large Structures]]
[[Category: Hibi, T.]]
[[Category: Hibi T]]
[[Category: Katano, H.]]
[[Category: Katano H]]
[[Category: Kurokawa, Y.]]
[[Category: Kurokawa Y]]
[[Category: Nakayama, M.]]
[[Category: Nakayama M]]
[[Category: Nii, H.]]
[[Category: Nii H]]
[[Category: Oda, J.]]
[[Category: Oda J]]
[[Category: Glutathione homeostasis]]
[[Category: Peptide synthesis]]
[[Category: Phosphoryl transfer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:35:15 2009''
Retrieved from "https://proteopedia.org/2d33"