This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3k7d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:28, 1 November 2017

C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase

Structural highlights

3k7d is a 2 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.
Ligands:
Related:	1v4a
Gene:	b3053, glnE, JW3025 ("Bacillus coli" Migula 1895)
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

The 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

↑ 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, Carr PD, Vasudevan SG, Ollis DL. Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: evidence for gene duplication and evolution of a new active site. J Mol Biol. 2010 Feb 26;396(3):773-84. Epub 2009 Dec 21. PMID:20026075 doi:10.1016/j.jmb.2009.12.011

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/3k7d"

@@ Line 1: / Line 1: @@
 ==C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase==
 <StructureSection load='3k7d' size='340' side='right' caption='[[3k7d]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b3053, glnE, JW3025 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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='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=3k7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7d OCA], [http://pdbe.org/3k7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k7d RCSB], [http://www.ebi.ac.uk/pdbsum/3k7d PDBsum]</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=3k7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7d OCA], [http://pdbe.org/3k7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k7d RCSB], [http://www.ebi.ac.uk/pdbsum/3k7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7d ProSAT]</span></td></tr>
 </table>
 == Function ==

3k7d

From Proteopedia

Revision as of 08:28, 1 November 2017

C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox