1ct9

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

Structural highlights

1ct9 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASNB_ECOLI Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Boehlein SK, Richards NG, Schuster SM. Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. J Biol Chem. 1994 Mar 11;269(10):7450-7. PMID:7907328
↑ Humbert R, Simoni RD. Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli. J Bacteriol. 1980 Apr;142(1):212-20. PMID:6102982
↑ Meyer ME, Gutierrez JA, Raushel FM, Richards NG. A conserved glutamate controls the commitment to acyl-adenylate formation in asparagine synthetase. Biochemistry. 2010 Nov 2;49(43):9391-401. doi: 10.1021/bi1010688. PMID:20853825 doi:http://dx.doi.org/10.1021/bi1010688

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Boehlein SK, Richards NG, Schuster SM. Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. J Biol Chem. 1994 Mar 11;269(10):7450-7. PMID:7907328

[2] Humbert R, Simoni RD. Genetic and biomedical studies demonstrating a second gene coding for asparagine synthetase in Escherichia coli. J Bacteriol. 1980 Apr;142(1):212-20. PMID:6102982

[3] Meyer ME, Gutierrez JA, Raushel FM, Richards NG. A conserved glutamate controls the commitment to acyl-adenylate formation in asparagine synthetase. Biochemistry. 2010 Nov 2;49(43):9391-401. doi: 10.1021/bi1010688. PMID:20853825 doi:http://dx.doi.org/10.1021/bi1010688

[1]

[2]

[3]

1ct9

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

Structural highlights

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

1ct9

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

Structural highlights

Function

Evolutionary Conservation

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search