7WGK

Crystal structure of Adenosine triphosphate phosphoribosyltransferase (HisG) from Acinetobacter baumannii at 3.13 A resolution

Summary for 7WGK

• Entry DOI: 10.2210/pdb7wgk/pdb
• Descriptor: ATP phosphoribosyltransferase (2 entities in total)
• Functional Keywords: catalytic domain of atp-prt, hisg, transferase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 2
• Total formula weight: 50226.41

Authors

Ahmad, N.,Maurya, A.,Singh, P.K.,Viswanathan, V.,Sharma, P.,Singh, T.P.,Sharma, S. (deposition date: 2021-12-28, release date: 2022-01-19, Last modification date: 2026-07-22)

Primary citation

Ahmad, N.,Sharma, P.,Sharma, S.,Singh, T.P.
Structure of the short-form ATP-phosphoribosyltransferase from Acinetobacter baumannii reveals the presence of a novel Mg 2+ sequestering and storage site.
Biochim Biophys Acta Proteins Proteom, 1874:141159-141159, 2026

PubMed Abstract: Adenosine triphosphate phosphoribosyltransferase (ATP-PRT), a member of the phosphoribosyltransferase (PRT) superfamily of enzymes, catalyses the first step in the histidine biosynthesis pathway, which involves the nucleophilic substitution of ATP onto phosphoribosyl pyrophosphate (PRPP) to generate phosphoribosyl-ATP (PR-ATP) and pyrophosphate (PP). The three-dimensional structure of short-form ATP-PRT from Acinetobacter baumannii (AbHisG) was determined using the X-ray crystallographic method. The structure determination revealed two crystallographically independent molecules in the asymmetric unit that formed an antiparallel homodimer. In all the structures of HisG proteins reported so far, the N-terminal segment is either absent from the amino acid sequence or not observed in the structure. This is the first structure where the N-terminal segment has been clearly observed. However, the most remarkable observation pertains to observing a Mg ion in the structure with the help of the N-terminal segment, which is loosely held with six coordination linkages, out of which one contact is made to the carbonyl oxygen atom of Asn16 at an average distance of 2.06 Å, and the other five contacts were with water oxygen atoms at distances varying from 2.40 to 2.59 Å. All the coordinating water oxygen atoms were held in place by multiple hydrogen bonds from surrounding protein atoms. The relatively loose coordination environment of the Mg ion indicates temporary sequestration of Mg, which may be released during catalytic need.

PubMed: 42336071
DOI: 10.1016/j.bbapap.2026.141159

Experimental method

X-RAY DIFFRACTION (3.13 Å)