7M58

Crystal structure of N1, a member of cis-3-chloroacrylic acid dehalogenase (cis-CaaD) family


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Kinetic and Structural Analysis of Two Linkers in the Tautomerase Superfamily: Analysis and Implications.

Baas, B.J.Medellin, B.P.LeVieux, J.A.Erwin, K.Lancaster, E.B.Johnson Jr., W.H.Kaoud, T.S.Moreno, R.Y.de Ruijter, M.Babbitt, P.C.Zhang, Y.J.Whitman, C.P.

(2021) Biochemistry 60: 1776-1786

  • DOI: https://doi.org/10.1021/acs.biochem.1c00220
  • Primary Citation of Related Structures:  
    7M58, 7M59

  • PubMed Abstract: 

    The tautomerase superfamily (TSF) is a collection of enzymes and proteins that share a simple β-α-β structural scaffold. Most members are constructed from a single-core β-α-β motif or two consecutively fused β-α-β motifs in which the N-terminal proline (Pro-1) plays a key and unusual role as a catalytic residue. The cumulative evidence suggests that a gene fusion event took place in the evolution of the TSF followed by duplication (of the newly fused gene) to result in the diversification of activity that is seen today. Analysis of the sequence similarity network (SSN) for the TSF identified several linking proteins ("linkers") whose similarity links subgroups of these contemporary proteins that might hold clues about structure-function relationship changes accompanying the emergence of new activities. A previously uncharacterized pair of linkers (designated N1 and N2) was identified in the SSN that connected the 4-oxalocrotonate tautomerase (4-OT) and cis -3-chloroacrylic acid dehalogenase ( cis -CaaD) subgroups. N1, in the cis -CaaD subgroup, has the full complement of active site residues for cis -CaaD activity, whereas N2, in the 4-OT subgroup, lacks a key arginine (Arg-39) for canonical 4-OT activity. Kinetic characterization and nuclear magnetic resonance analysis show that N1 has activities observed for other characterized members of the cis -CaaD subgroup with varying degrees of efficiencies. N2 is a modest 4-OT but shows enhanced hydratase activity using allene and acetylene compounds, which might be due to the presence of Arg-8 along with Arg-11. Crystallographic analysis provides a structural context for these observations.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tautomerase_3 domain-containing protein
A, B, C
144Corynebacterium halotolerans YIM 70093 = DSM 44683Mutation(s): 0 
Gene Names: A605_05910
UniProt
Find proteins for M1NLA4 (Corynebacterium halotolerans YIM 70093 = DSM 44683)
Explore M1NLA4 
Go to UniProtKB:  M1NLA4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupM1NLA4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.263 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.202 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.362α = 90
b = 87.822β = 90
c = 120.71γ = 90
Software Package:
Software NamePurpose
HKL-2000data scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)GM-129331
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)GM-104896
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)GM125882
Robert A. Welch FoundationF-1778

Revision History  (Full details and data files)

  • Version 1.0: 2021-06-02
    Type: Initial release
  • Version 1.1: 2021-06-23
    Changes: Database references
  • Version 1.2: 2023-10-18
    Changes: Data collection, Database references, Refinement description