1ixi

PHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 56 REPLACED BY ASN COMPLEX WITH MONOBASIC PHOSPHATE IONPHOSPHATE-BINDING PROTEIN MUTANT WITH ASP 56 REPLACED BY ASN COMPLEX WITH MONOBASIC PHOSPHATE ION

Structural highlights

1ixi is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	POTENTIAL (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PSTS_ECOLI] Part of the ABC transporter complex PstSACB involved in phosphate import.

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

A very short hydrogen bond between an Asp and a phosphate is established in two high resolution structures (0.98 and 1.05 A). A mutant complex that changes the Asp to an Asn, which forms a normal hydrogen bond, has a similar free energy of binding to the wild type complex, suggesting that the contribution of the short hydrogen bond is not extraordinarily strong.

A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes.,Wang Z, Luecke H, Yao N, Quiocho FA Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942^[1]

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

References

↑ Wang Z, Luecke H, Yao N, Quiocho FA. A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942

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OCA

[1] Wang Z, Luecke H, Yao N, Quiocho FA. A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes. Nat Struct Biol. 1997 Jul;4(7):519-22. PMID:9228942

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