3k7d: Difference between revisions
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==C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase== | ==C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase== | ||
<StructureSection load='3k7d' size='340' side='right' caption='[[3k7d]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3k7d' size='340' side='right'caption='[[3k7d]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3k7d]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3k7d]] 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=3K7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K7D FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7d OCA], [https://pdbe.org/3k7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k7d RCSB], [https://www.ebi.ac.uk/pdbsum/3k7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7d ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GLNE_ECOLI GLNE_ECOLI] Adenylation and deadenylation of glutamate--ammonia ligase.<ref>PMID:8412694</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/3k7d_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/3k7d_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 35: | Line 33: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Carr PD]] | ||
[[Category: | [[Category: Ollis DL]] | ||
[[Category: | [[Category: Vasudevan SG]] | ||
[[Category: | [[Category: Xu Y]] | ||
Latest revision as of 11:10, 6 September 2023
C-terminal (adenylylation) domain of E.coli Glutamine Synthetase AdenylyltransferaseC-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase
Structural highlights
FunctionGLNE_ECOLI Adenylation and deadenylation of glutamate--ammonia ligase.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe X-ray structure of the C-terminal fragment, containing residues 449-946, of Escherichia coli glutamine synthetase adenylyl transferase (ATase) has been determined. ATase is part of the cascade that regulates the enzymatic activity of E. coli glutamine synthetase, a key component of the cell's machinery for the uptake of ammonia. It has two enzymatic activities, adenylyl removase (AR) and adenylyl transferase (AT), which are located in distinct catalytic domains that are separated by a regulatory (R) domain. We previously reported the three-dimensional structure of the AR domain (residues 1-440). The present structure contains both the R and AT domains. AR and AT share 24% sequence identity and also contain the beta-polymerase motif that is characteristic of many nucleotidylyl transferase enzymes. The structures overlap with an rmsd of 2.4 A when the superhelical R domain is omitted. A model for the complete ATase molecule is proposed, along with some refinements of domain boundaries. A rather more speculative model for the complex of ATase with glutamine synthetase and the nitrogen signal transduction protein PII is also presented. Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: evidence for gene duplication and evolution of a new active site.,Xu Y, Carr PD, Vasudevan SG, Ollis DL J Mol Biol. 2010 Feb 26;396(3):773-84. Epub 2009 Dec 21. PMID:20026075[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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