1ger: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1ger.png|left|200px]]


<!--
==THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES==
The line below this paragraph, containing "STRUCTURE_1ger", creates the "Structure Box" on the page.
<StructureSection load='1ger' size='340' side='right'caption='[[1ger]], [[Resolution|resolution]] 1.86&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'>[[1ger]] 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=1GER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GER 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]] 1.86&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
{{STRUCTURE_1ger|  PDB=1ger  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ger FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ger OCA], [https://pdbe.org/1ger PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ger RCSB], [https://www.ebi.ac.uk/pdbsum/1ger PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ger ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSHR_ECOLI GSHR_ECOLI] Maintains high levels of reduced glutathione in the cytosol.
== 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/ge/1ger_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=1ger ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the dimeric flavoenzyme glutathione reductase from Escherichia coli was determined and refined to an R-factor of 16.8% at 1.86 A resolution. The molecular 2-fold axis of the dimer is local but very close to a possible crystallographic 2-fold axis; the slight asymmetry could be rationalized from the packing contacts. The 2 crystallographically independent subunits of the dimer are virtually identical, yielding no structural clue on possible cooperativity. The structure was compared with the well-known structure of the homologous enzyme from human erythrocytes with 52% sequence identity. Significant differences were found at the dimer interface, where the human enzyme has a disulfide bridge, whereas the E. coli enzyme has an antiparallel beta-sheet connecting the subunits. The differences at the glutathione binding site and in particular a deformation caused by a Leu-Ile exchange indicate why the E. coli enzyme accepts trypanothione much better than the human enzyme. The reported structure provides a frame for explaining numerous published engineering results in detail and for guiding further ones.


===THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES===
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.,Mittl PR, Schulz GE Protein Sci. 1994 May;3(5):799-809. PMID:8061609<ref>PMID:8061609</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ger" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_8061609}}, adds the Publication Abstract to the page
*[[Glutathione Reductase|Glutathione Reductase]]
(as it appears on PubMed at http://www.pubmed.gov), where 8061609 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_8061609}}
__TOC__
 
</StructureSection>
==About this Structure==
1GER 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=1GER OCA].
 
==Reference==
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes., Mittl PR, Schulz GE, Protein Sci. 1994 May;3(5):799-809. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8061609 8061609]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutathione-disulfide reductase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Mittl PRE]]
[[Category: Mittl, P R.E.]]
[[Category: Schulz GE]]
[[Category: Schulz, G E.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:10:47 2008''

Latest revision as of 07:22, 23 October 2024

THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES

1ger, resolution 1.86Å

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=1ger&oldid=4233883"