The histidine triad superfamily of nucleotide-binding proteins
نویسندگان
چکیده
منابع مشابه
The histidine triad superfamily of nucleotide-binding proteins.
Histidine triad (HIT) proteins were until recently a superfamily of proteins that shared only sequence motifs. Crystal structures of nucleotide-bound forms of histidine triad nucleotide-binding protein (Hint) demonstrated that the conserved residues in HIT proteins are responsible for their distinctive, dimeric, 10-stranded half-barrel structures that form two identical purine nucleotide-bindin...
متن کاملStructural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamily.
The histidine triad proteins (HITs) constitute a large and ubiquitous superfamily of nucleotide hydrolases. The human histidine triad nucleotide-binding proteins (hHints) are a distinct class of HITs noted for their acyl-AMP hydrolase and phosphoramidase activity. The first high-resolution crystal structures of hHint2 with and without bound AMP are described. The differences between hHint2 and ...
متن کاملKinetic mechanism of human histidine triad nucleotide binding protein 1.
Human histidine triad nucleotide binding protein 1 (hHint1) is a member of a ubiquitous and ancient branch of the histidine triad protein superfamily. hHint1 is a homodimeric protein that catalyzes the hydrolysis of model substrates, phosphoramidate and acyl adenylate, with a high efficiency. Recently, catalytically inactive hHint1 has been identified as the cause of inherited peripheral neurop...
متن کاملFHIT (fragile histidine triad)
Fhit protein is a tumor suppressor with reduced or no expression in many types of cancer. Fhit expression is more frequently lost in cancers of individuals with familial mutations causing deficiency in DNA repair genes such as BRCA1 and BRCA2 and MSH2. In vitro Fhit acts as a hydrolase that cleaves diadenosine triphosphate (Ap3A) to ADP and AMP. The Fhit-Ap3A enzyme-substrate complex appears to...
متن کاملComponents of histidine transport: histidine-binding proteins and hisP protein.
The high-affinity (K(m) = 3 x 10(-8) M) transport system for histidine in Salmonella typhimurium has been resolved into three components: J, K, and P. J, which is a histidine-binding protein released by osmotic shock, is specified by the hisJ gene: hisJ mutants lack the binding protein and are defective in histidine transport. Another class of mutants-dhuA, which is closely linked to hisJ-has f...
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ژورنال
عنوان ژورنال: Journal of Cellular Physiology
سال: 1999
ISSN: 0021-9541,1097-4652
DOI: 10.1002/(sici)1097-4652(199911)181:2<179::aid-jcp1>3.0.co;2-8