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1v4a

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Revision as of 06:24, 6 October 2021

Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase

Structural highlights

1v4a is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Activity:	[Glutamate--ammonia-ligase_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number 2.7.7.42
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GLNE_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 PubMed

We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.

Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.,Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL Structure. 2004 May;12(5):861-9. PMID:15130478^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Heeswijk WC, Rabenberg M, Westerhoff HV, Kahn D. The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol Microbiol. 1993 Aug;9(3):443-57. PMID:8412694
↑ Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure. 2004 May;12(5):861-9. PMID:15130478 doi:10.1016/j.str.2004.02.029

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v4a"

@@ Line 3: / Line 3: @@
 <StructureSection load='1v4a' size='340' side='right'caption='[[1v4a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1v4a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V4A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1v4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V4A FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Glutamate--ammonia-ligase]_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.42 2.7.7.42] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/[Glutamate--ammonia-ligase]_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.42 2.7.7.42] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4a OCA], [http://pdbe.org/1v4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v4a RCSB], [http://www.ebi.ac.uk/pdbsum/1v4a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v4a ProSAT]</span></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=1v4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4a OCA], [https://pdbe.org/1v4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v4a RCSB], [https://www.ebi.ac.uk/pdbsum/1v4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v4a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLNE_ECOLI GLNE_ECOLI]] Adenylation and deadenylation of glutamate--ammonia ligase.<ref>PMID:8412694</ref>
+[[https://www.uniprot.org/uniprot/GLNE_ECOLI GLNE_ECOLI]] Adenylation and deadenylation of glutamate--ammonia ligase.<ref>PMID:8412694</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1v4a

From Proteopedia

Revision as of 06:24, 6 October 2021

Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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