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. 2013 Dec 24;70(Pt 1):79–90. doi: 10.1107/S1399004713024838

Table 3. Structural analysis of the molecular footprint of BrsV.

Mutation Protein region Structural explanation
C70A Active site Structural stabilization of active site by a disulfide bridge
R119A N-terminal insertion Arg119 is involved in salt-bridge interactions allowing N-­terminal insertion in BsrV
R121A N-terminal insertion Arg121 is involved in salt-bridge interactions allowing N-­terminal insertion in BsrV
A165K Active site Ala at this position allows the correct stabilization of the Cl ion by Arg173 and Asn174 (in Alrs, this position is occupied by the N-carboxylated Lys)
N167A Active site Structural stabilization of loop involved in Cl coordination
G169A Active site Loop involved in Cl coordination
N174A Active site Residue involved in Cl coordination
P206N Entry loops Structural stabilization of the L1 loop (involved in substrate entry)
Y208A Entry loops Stabilization of the PLP phosphate group
K216A Entry loops Salt-bridge interaction stabilizing α10 at the entry
Y246A Entry loops Mutation will block movement of the r2 region
G263I Active site Gly residue allows Asp268 and Tyr394 stabilization of side chains of different substrates
N348A Active site Stabilization of loop that includes Met347 at the catalytic site
T349A Active site
P391N Active site This Pro is critical in the broad specificity of BsrV, allowing the stabilization of side chains from different substrates