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PDBsum entry 2frf
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protein ligands links
Oxygen storage/transport PDB id
2frf

 

 

 

 

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Contents
Protein chain
152 a.a. *
Ligands
SO4 ×2
NO2-HEM
Waters ×187
* Residue conservation analysis
PDB id:
2frf
Name: Oxygen storage/transport
Title: Horse heart myoglobin, nitrite adduct, crystal soak
Structure: Myoglobin. Chain: a
Source: Equus caballus. Horse. Organism_taxid: 9796. Other_details: heart muscle
Resolution:
1.20Å     R-factor:   0.170     R-free:   0.211
Authors: D.M.Copeland,A.S.Soares,A.H.West,G.B.Richter-Addo
Key ref: D.M.Copeland et al. (2006). Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin. J Inorg Biochem, 100, 1413-1425. PubMed id: 16777231 DOI: 10.1016/j.jinorgbio.2006.04.011
Date:
19-Jan-06     Release date:   30-May-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P68082  (MYG_HORSE) -  Myoglobin from Equus caballus
Seq:
Struc: 		154 a.a.
152 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.jinorgbio.2006.04.011 J Inorg Biochem 100:1413-1425 (2006)
PubMed id: 16777231  
 
 
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin.
D.M.Copeland, A.S.Soares, A.H.West, G.B.Richter-Addo.
 
  ABSTRACT  
 
Nitrite is an important species in the global nitrogen cycle, and the nitrite reductase enzymes convert nitrite to nitric oxide (NO). Recently, it has been shown that hemoglobin and myoglobin catalyze the reduction of nitrite to NO under hypoxic conditions. We have determined the 1.20 A resolution crystal structure of the nitrite adduct of ferric horse heart myoglobin (hh Mb). The ligand is bound to iron in the nitrito form, and the complex is formulated as MbIII(ONO-). The Fe-ONO bond length is 1.94 A, and the O-N-O angle is 113 degrees . In addition, the nitrite ligand is stabilized by hydrogen bonding with the distal His64 residue. We have also determined the 1.30 A resolution crystal structures of hh MbIINO. When hh MbIINO is prepared from the reaction of metMbIII with nitrite/dithionite, the FeNO angle is 144 degrees with a Fe-NO bond length of 1.87 A. However, when prepared from the reaction of NO with reduced MbII, the FeNO angle is 120 degrees with a Fe-NO bond length of 2.13 A. This difference in FeNO conformations as a function of preparative method is reproducible, and suggests a role of the distal pocket in hh MbIINO in stabilizing local FeNO conformational minima.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21067516 N.T.Hunt, G.M.Greetham, M.Towrie, A.W.Parker, and N.P.Tucker (2011).
Relationship between protein structural fluctuations and rebinding dynamics in ferric haem nitrosyls.
  Biochem J, 433, 459-468.  
21425285 Y.Liu, and H.Sun (2011).
Electronic ground states and vibrational frequency shifts of diatomic ligands in heme adducts.
  J Comput Chem, 32, 1279-1285.  
19705829 J.Su, and J.T.Groves (2009).
Direct detection of the oxygen rebound intermediates, ferryl Mb and NO2, in the reaction of metmyoglobin with peroxynitrite.
  J Am Chem Soc, 131, 12979-12988.  
19924902 J.Yi, J.Heinecke, H.Tan, P.C.Ford, and G.B.Richter-Addo (2009).
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
  J Am Chem Soc, 131, 18119-18128.
PDB codes: 3hc9 3hen 3heo 3hep
18274790 C.Xu, and G.S.Thomas (2008).
Ambidentate H-bonding by heme-bound NO: structural and spectral effects of -O versus -N H-bonding.
  J Biol Inorg Chem, 13, 613-621.  
18388202 P.R.Castello, D.K.Woo, K.Ball, J.Wojcik, L.Liu, and R.O.Poyton (2008).
Oxygen-regulated isoforms of cytochrome c oxidase have differential effects on its nitric oxide production and on hypoxic signaling.
  Proc Natl Acad Sci U S A, 105, 8203-8208.  
17905436 Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, and G.B.Richter-Addo (2008).
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.
  J Inorg Biochem, 102, 216-233.
PDB codes: 2o58 2o5b 2o5l 2o5m 2o5o 2o5q 2o5s 2o5t
17488722 E.R.Schreiter, M.M.Rodríguez, A.Weichsel, W.R.Montfort, and J.Bonaventura (2007).
S-nitrosylation-induced conformational change in blackfin tuna myoglobin.
  J Biol Chem, 282, 19773-19780.
PDB codes: 2nrl 2nrm 2nx0
17982448 S.Basu, R.Grubina, J.Huang, J.Conradie, Z.Huang, A.Jeffers, A.Jiang, X.He, I.Azarov, R.Seibert, A.Mehta, R.Patel, S.B.King, N.Hogg, A.Ghosh, M.T.Gladwin, and D.B.Kim-Shapiro (2007).
Catalytic generation of N2O3 by the concerted nitrite reductase and anhydrase activity of hemoglobin.
  Nat Chem Biol, 3, 785-794.  
17215864 X.Ma, N.Sayed, A.Beuve, and F.van den Akker (2007).
NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism.
  EMBO J, 26, 578-588.
PDB codes: 2o09 2o0c 2o0g
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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