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![[Figure 4]](chr5006fig4mag.jpg)
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Figure 4
Overlay of the structure of SABP2 with a bound product salicylate (PDB entry 1y7i, blue C atoms) onto the structure of HNL40 with a bound proline (PDB entry 8sni, yellow C atoms). The carboxylate moieties interact with the corresponding protein active sites slightly differently. The catalytic serine donates hydrogen bonds (not shown) to both salicylate carboxylate O atoms (3.0 and 3.0 Å) in the SABP2 structure, but the altered catalytic serine side-chain conformation in the HNL40 structure makes the angle too acute for the serine to donate a hydrogen bond to the proline carboxylate even though the O–O distance is still favorable (3.0 and 3.0 Å). Instead, the one proline carboxylate O atom accepts a hydrogen bond from a nearby water molecule (2.8 Å) and the proline ammonium donates a weak hydrogen bond to the catalytic serine (3.3 Å). |
![[Figure 4]](chr5006fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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