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![[Figure 4]](rr5021fig4mag.jpg)
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Figure 4
The positions of the phenylalanine residues equivalent to Phe336 in MlFabH found in Gram-negative bacteria occupy the binding site for the branched acyl-CoA group. Modeling analysis and the docking of a substrate (lauroyl-coenzyme A) into the active site of MlFabH shows that residue Phe336, which is located close to the catalytic triad, has a completely different orientation compared with residue Phe304 of the Gram-negative E. coli FabH. The position of Phe336 is influenced by the surrounding Trp246 residue via hydrophobic contacts. The residue equivalent to Trp246 in MlFabH in the Gram-negative EcFabH is Val215, which allows the conserved phenylalanine residue to assume a different rotamer orientation compared with MlFabH. |
![[Figure 4]](rr5021fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
