The Open Protein Structure Annotation Network
PDB Keyword


    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes. Acta Crystallogr.,Sect.F 66 1317-1325 2010
    Site JCSG
    PDB Id 2pv7 Target Id 374967
    Molecular Characteristics
    Source Haemophilus influenzae rd kw20
    Alias Ids TPS1637,1574749, PF02153 Molecular Weight 33804.87 Da.
    Residues 297 Isoelectric Point 5.42
    Sequence mresyanenqfgfktinsdihkivivggygklgglfarylrasgypisildredwavaesilanadvvi vsvpinltletierlkpyltenmlladltsvkreplakmlevhtgavlglhpmfgadiasmakqvvvrc dgrfperyewlleqiqiwgakiyqtnatehdhnmtyiqalrhfstfanglhlskqpinlanllalsspi yrlelamigrlfaqdaelyadiimdksenlavietlkqtydealtffenndrqgfidafhkvrdwfgdy seqflkesrqllqqandlkqg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.00 Rfree 0.194
    Matthews' coefficent 2.98 Rfactor 0.161
    Waters 393 Solvent Content 58.72

    Ligand Information


    Google Scholar output for 2pv7
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
    2. The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes
    HJ Chiu, P Abdubek, T Astakhova - Section F: Structural , 2010 - scripts.iucr.org
    3. Crystal structure of prephenate dehydrogenase from Streptococcus mutans
    HK Ku, NH Do, JS Song, S Choi, SH Yeon - International journal of , 2011 - Elsevier
    4. Hidden Relationship between Conserved Residues and Locally Conserved Phosphate-Binding Structures in NAD (P)-Binding Proteins
    CY Wu, YH Hwa, YC Chen, C Lim - The Journal of Physical , 2012 - ACS Publications

    Protein Summary

    The tirA(HI1290) gene encodes a 377 residues long sequence (NP_439442.1) that functions as a bifunctional chorismate mutase/prephenate dehydrogenase. This enzyme is involved in the Tyr biosynthesis catalyzing the conversion of chorismate to prephenate (EC: and subsequently to 4-OH-phenyl-pyruvate using NAD as cofactor (EC: The final product of the pathway, Tyr, is a negative regulator. The full length sequence includes 2 domains. The N-terminal (1-110) belongs to the chorismate mutase type 2 (PF01817) characterized by the conservation of residues R10-R28-E88. The C-terminal fragment (110-377) contains the prephenate dehydrogenase activity (PF02153) identifiable by the conserved pattern of residues D146-P153-()-D176-S179-K181-()-P201-G204-S209-()-H248-D249-()-R297-K313. In its genome vicinity, the chorismate synthase aroC (YP_001290292) is found with a 0.931 STRING score.  


    2pv7 structure corresponds to the C-terminal fragment (81-377) of this protein. Its crystal homodimer shows 1 NAD molecule per chain in contact with regions K111-L112, D131-R132-W135, V152-P153, S179, P201-G204. Also 1 Tyr molecule per chain is observed in the vicinity of residues S179, H200-P201-G204, R297. SCOP divides 2pv7 coordinates in two regions: 92-243 region belongs to the alpha/beta class, NAD-binding Rossmann fold superfamily, 6-phosphogluconate dehydrogenase N-terminal domain-like family; 244-371 region belongs to the all-alpha class, 6-phosphogluconate dehydrogenase C-terminal domain-like superfamily, TyrA dimerization domain-like family. Significant structural neighbors (FFAS scr=-60; HHpred P-val=3e-28; SSM 80%; Dali Z-scr=20; FATCAT P-val=2e-6) are 2f1k [Ref], 2g5c [Ref], and 3ggg [Ref], all prephenate dehydrogenases.

    Ligand Summary





    1. (No Results)


      Discuss this publication
    2. (No Results)


      Discuss this publication
    3. (No Results)


      Discuss this publication

    Files (0)

    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch