2fpr

[[Image:2fpr.jpg|left|200px]]

|PDB= 2fpr |SIZE=350|CAPTION= <scene name='initialview01'>2fpr</scene>, resolution 1.70&Aring;

|SITE=

|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=BR:BROMIDE ION'>BR</scene>

|ACTIVITY= [http://en.wikipedia.org/wiki/Histidinol-phosphatase Histidinol-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.15 3.1.3.15]

|GENE= hisB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])

 

 

 

HisB from Escherichia coli is a bifunctional enzyme catalyzing the sixth and eighth steps of l-histidine biosynthesis. The N-terminal domain (HisB-N) possesses histidinol phosphate phosphatase activity, and its crystal structure shows a single domain with fold similarity to the haloacid dehalogenase (HAD) enzyme family. HisB-N forms dimers in the crystal and in solution. The structure shows the presence of a structural Zn(2+) ion stabilizing the conformation of an extended loop. Two metal binding sites were also identified in the active site. Their presence was further confirmed by isothermal titration calorimetry. HisB-N is active in the presence of Mg(2+), Mn(2+), Co(2+), or Zn(2+), but Ca(2+) has an inhibitory effect. We have determined structures of several intermediate states corresponding to snapshots along the reaction pathway, including that of the phosphoaspartate intermediate. A catalytic mechanism, different from that described for other HAD enzymes, is proposed requiring the presence of the second metal ion not found in the active sites of previously characterized HAD enzymes, to complete the second half-reaction. The proposed mechanism is reminiscent of two-Mg(2+) ion catalysis utilized by DNA and RNA polymerases and many nucleases. The structure also provides an explanation for the inhibitory effect of Ca(2+).

 

2FPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPR OCA].

 

==Reference==

Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway., Rangarajan ES, Proteau A, Wagner J, Hung MN, Matte A, Cygler M, J Biol Chem. 2006 Dec 8;281(49):37930-41. Epub 2006 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16966333 16966333]

[[Category: Histidinol-phosphatase]]

[[Category: Single protein]]

[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]

[[Category: Rangarajan, E S.]]

[[Category: BR]]

[[Category: MG]]

[[Category: NA]]

[[Category: bifunctional enzyme.]]

[[Category: bsgi]]

[[Category: hisb]]

[[Category: histidinola phosphate phosphatase]]

[[Category: montreal-kingston bacterial structural genomics initiative]]

[[Category: structural genomic]]