Literature summary for 1.5.3.1 extracted from

Jorns, M.S.; Chen, Z.W.; Mathews, F.S.
Structural characterization of mutations at the oxygen activation site in monomeric sarcosine oxidase (2010), Biochemistry, 49, 3631-3639.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus sp. (in: Bacteria)

Crystallization (Commentary)

Crystallization (Comment)	Organism
mutants K265M, K265Q, K265A, K265R, to 1.6-2.1 A resolution. The overall structure of MSOX and residue conformation in the sarcosine binding cavity are unaffected by replacement of K265 with Met or Arg. The side chain of K265M exhibits the same configuration in each molecule of K265M crystals and is nearly congruent with K265 in wild-type MSOX. The side chain of K265R is dramatically shifted compared with K265, points in the opposite direction, and exhibits significant conformational variability between molecules of the same crystal. The major species in solutions of K265R is likely to contain a flipped-out R265 and exhibit negligible oxygen activation, similar to K265M. The 400fold higher oxygen reactivity observed with K265R is attributed to a minor flipped-in R265 conformer whose oxygen reactivity is similar to that of wild-type MSOX. Structural water molecule 1 is strikingly absent in K265M and K265R	Bacillus sp. (in: Bacteria)

Crystallization (Comment)

Organism

mutants K265M, K265Q, K265A, K265R, to 1.6-2.1 A resolution. The overall structure of MSOX and residue conformation in the sarcosine binding cavity are unaffected by replacement of K265 with Met or Arg. The side chain of K265M exhibits the same configuration in each molecule of K265M crystals and is nearly congruent with K265 in wild-type MSOX. The side chain of K265R is dramatically shifted compared with K265, points in the opposite direction, and exhibits significant conformational variability between molecules of the same crystal. The major species in solutions of K265R is likely to contain a flipped-out R265 and exhibit negligible oxygen activation, similar to K265M. The 400fold higher oxygen reactivity observed with K265R is attributed to a minor flipped-in R265 conformer whose oxygen reactivity is similar to that of wild-type MSOX. Structural water molecule 1 is strikingly absent in K265M and K265R

Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants	Comment	Organism
K265A	at least 250fold decrease in reaction rate. Crystallization analysis	Bacillus sp. (in: Bacteria)
K265M	at least 250fold decrease in reaction rate. Crystallization analysis	Bacillus sp. (in: Bacteria)
K265Q	at least 250fold decrease in reaction rate. Crystallization analysis	Bacillus sp. (in: Bacteria)
K265R	at least 250fold decrease in reaction rate. Crystallization analysis	Bacillus sp. (in: Bacteria)

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	P40859	-	-
Bacillus sp. (in: Bacteria) B-0618	P40859	-	-