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PDBsum entry 1keq
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protein ligands metals links
Lyase PDB id
1keq

 

 

 

 

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Contents
Protein chains
238 a.a. *
Ligands
4MZ ×5
ACY ×3
Metals
__K
_ZN ×2
Waters ×471
* Residue conservation analysis
PDB id:
1keq
Name: Lyase
Title: Crystal structure of f65a/y131c carbonic anhydrase v, covalently modified with 4-chloromethylimidazole
Structure: F65a/y131c-mi carbonic anhydrase v. Chain: a, b. Fragment: carbonic anhydrase vc. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: mca5c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Not given
Resolution:
1.88Å     R-factor:   0.185     R-free:   0.217
Authors: K.M.Jude,S.K.Wright,C.Tu,D.N.Silverman,R.E.Viola,D.W.Christianson
Key ref:
K.M.Jude et al. (2002). Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle. Biochemistry, 41, 2485-2491. PubMed id: 11851394 DOI: 10.1021/bi015808q
Date:
16-Nov-01     Release date:   06-Mar-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P23589  (CAH5A_MOUSE) -  Carbonic anhydrase 5A, mitochondrial from Mus musculus
Seq:
Struc: 		299 a.a.
238 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - carbonic anhydrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: hydrogencarbonate + H+ = CO2 + H2O
hydrogencarbonate
 + H(+)
 =
CO2
Bound ligand (Het Group name = ACY)
matches with 75.00% similarity 		+ H2O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1021/bi015808q Biochemistry 41:2485-2491 (2002)
PubMed id: 11851394  
 
 
Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle.
K.M.Jude, S.K.Wright, C.Tu, D.N.Silverman, R.E.Viola, D.W.Christianson.
 
  ABSTRACT  
 
The crystal structure of F65A/Y131C murine alpha-carbonic anhydrase V (CAV), covalently modified at cysteine residues with 4-chloromethylimidazole, is reported at 1.88 A resolution. This modification introduces a methylimidazole (MI) group at residue C131 in the active site with important consequences. F65A/Y131C-MI CAV exhibits an up to 3-fold enhancement of catalytic activity over that of wild-type CAV [Earnhardt, J. N., Wright, S. K., Qian, M., Tu, C., Laipis, P. J., Viola, R. E., and Silverman, D. N. (1999) Arch. Biochem. Biophys. 361, 264-270]. In this modified CAV variant, C131-MI acts as a proton shuttle, facilitating the deprotonation of a zinc-bound water molecule to regenerate the nucleophilic zinc-bound hydroxide ion. A network of three hydrogen-bonded water molecules, across which proton transfer likely proceeds, bridges the zinc-bound water molecule and the C131-MI imidazole group. The structure of F65A/Y131C-MI CAV is compared to structures of Y64H/F65A murine CAV, wild-type human alpha-carbonic anhydrase II, and the gamma-carbonic anhydrase from Methanosarcina thermophilain an effort to outline common features of catalytic proton shuttles.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21152508 B.Li, S.Q.Zang, C.Ji, C.X.Du, H.W.Hou, and T.C.Mak (2011).
Syntheses, structures and properties of two unusual silver-organic coordination networks: 1D→1D tubular intertwinement and existence of an infinite winding water chain.
  Dalton Trans, 40, 788-792.  
19679199 R.L.Mikulski, and D.N.Silverman (2010).
Proton transfer in catalysis and the role of proton shuttles in carbonic anhydrase.
  Biochim Biophys Acta, 1804, 422-426.  
18942852 J.Zheng, B.S.Avvaru, C.Tu, R.McKenna, and D.N.Silverman (2008).
Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II.
  Biochemistry, 47, 12028-12036.
PDB codes: 3dv7 3dvb 3dvc 3dvd
18335973 V.M.Krishnamurthy, G.K.Kaufman, A.R.Urbach, I.Gitlin, K.L.Gudiksen, D.B.Weibel, and G.M.Whitesides (2008).
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
  Chem Rev, 108, 946.  
17071654 D.Bhatt, S.Z.Fisher, C.Tu, R.McKenna, and D.N.Silverman (2007).
Location of binding sites in small molecule rescue of human carbonic anhydrase II.
  Biophys J, 92, 562-570.
PDB codes: 2fnk 2fnm 2fnn
17427958 I.Elder, Z.Fisher, P.J.Laipis, C.Tu, R.McKenna, and D.N.Silverman (2007).
Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III.
  Proteins, 68, 337-343.
PDB codes: 2hfw 2hfx 2hfy 3uyn 3uyq
17009455 P.Raghavaiah, S.Supriya, and S.K.Das (2006).
Sulfate anion helices formed by the assistance of a flip-flop water chain.
  Chem Commun (Camb), (), 2762-2764.  
17146506 S.Zang, Y.Su, C.Duan, Y.Li, H.Zhu, and Q.Meng (2006).
Coexistence of chiral hydrophilic and achiral hydrophobic channels in one multi-helical-array metal-organic framework incorporating helical water cluster chains.
  Chem Commun (Camb), (), 4997-4999.  
16526858 Y.C.Choi, C.Pak, and K.S.Kim (2006).
Electric field effects on water clusters (n = 3-5): systematic ab initio study of structures, energetics, and transition states.
  J Chem Phys, 124, 94308.  
16094479 M.S.Wang, G.C.Guo, M.L.Fu, L.Xu, L.Z.Cai, and J.S.Huang (2005).
Self-assembly of copper(ii) complexes with ladder, bi-rack, rack--ladder--rack and layer structures by the directional-bonding approach using a T-shaped ligand.
  Dalton Trans, (), 2899-2907.  
15281856 C.Manca, C.Tanner, S.Coussan, A.Bach, and S.Leutwyler (2004).
H atom transfer along an ammonia chain: tunneling and mode selectivity in 7-hydroxyquinoline.(NH3)3.
  J Chem Phys, 121, 2578-2590.  
12171926 C.Tu, M.Qian, H.An, N.R.Wadhwa, D.Duda, C.Yoshioka, Y.Pathak, R.McKenna, P.J.Laipis, and D.N.Silverman (2002).
Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase.
  J Biol Chem, 277, 38870-38876.
PDB code: 1lzv
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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