Sandbox Reserved 994: Difference between revisions

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== Structure ==

OXA-24 is a monomeric protein with an active site composed of a short α-helix and a β-sheet. The active site of OXA-24 is characterized by a hydrophobic pocket, which is representative of Class D β-lactamases as a whole. The hydrophobic bridge contributes to the substrate specificity for carbapenems and is composed of an arrangement of the Tyr-112 and Met-223 side chains.<ref name="Santillana">PMCID: PMC1838445</ref> These residues block the active site and only allow a very specific binding configuration of antibiotics. The active site is overall positively charged and contains a sulfate ion along with other solvent molecules when no substrate is bound. The mechanism of attack is through the use of three catalytic residues: Serine-81, Carboxylated Lysine-84, and Serine-128. <scene name='69/691536/Catalytic_residues_oxa24/1'>Catalytic Residues</scene> The hydroxyl chain of Ser-128 conforms in the direction of the active-serine Ser-81, and contributes to the catalytic mechanism.<ref name="Santillana" />

OXA-24 is a monomeric protein with an active site composed of a short α-helix and a β-sheet. The active site of OXA-24 is characterized by a hydrophobic pocket, which is representative of Class D β-lactamases as a whole. The hydrophobic bridge contributes to the substrate specificity for carbapenems and is composed of an arrangement of the Tyr-112 and Met-223 side chains.<ref name="Santillana">PMCID: PMC1838445</ref> <scene name='69/691536/Oxa24_bridge/1'>Bridge</scene> These residues block the active site and only allow a very specific binding configuration of antibiotics. The active site is overall positively charged and contains a sulfate ion along with other solvent molecules when no substrate is bound. The mechanism of attack is through the use of three catalytic residues: Serine-81, Carboxylated Lysine-84, and Serine-128. <scene name='69/691536/Catalytic_residues_oxa24/1'>Catalytic Residues</scene> The hydroxyl chain of Ser-128 conforms in the direction of the active-serine Ser-81, and contributes to the catalytic mechanism.<ref name="Santillana" />

== Hydrolysis Mechanism ==

Sandbox Reserved 994: Difference between revisions

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 == Structure ==
-OXA-24 is a monomeric protein with an active site composed of a short α-helix and a β-sheet. The active site of OXA-24 is characterized by a hydrophobic pocket, which is representative of Class D β-lactamases as a whole. The hydrophobic bridge contributes to the substrate specificity for carbapenems and is composed of an arrangement of the Tyr-112 and Met-223 side chains.<ref name="Santillana">PMCID: PMC1838445</ref> These residues block the active site and only allow a very specific binding configuration of antibiotics. The active site is overall positively charged and contains a sulfate ion along with other solvent molecules when no substrate is bound. The mechanism of attack is through the use of three catalytic residues: Serine-81, Carboxylated Lysine-84, and Serine-128. <scene name='69/691536/Catalytic_residues_oxa24/1'>Catalytic Residues</scene> The hydroxyl chain of Ser-128 conforms in the direction of the active-serine Ser-81, and contributes to the catalytic mechanism.<ref name="Santillana" />
+OXA-24 is a monomeric protein with an active site composed of a short α-helix and a β-sheet. The active site of OXA-24 is characterized by a hydrophobic pocket, which is representative of Class D β-lactamases as a whole. The hydrophobic bridge contributes to the substrate specificity for carbapenems and is composed of an arrangement of the Tyr-112 and Met-223 side chains.<ref name="Santillana">PMCID: PMC1838445</ref> <scene name='69/691536/Oxa24_bridge/1'>Bridge</scene> These residues block the active site and only allow a very specific binding configuration of antibiotics. The active site is overall positively charged and contains a sulfate ion along with other solvent molecules when no substrate is bound. The mechanism of attack is through the use of three catalytic residues: Serine-81, Carboxylated Lysine-84, and Serine-128. <scene name='69/691536/Catalytic_residues_oxa24/1'>Catalytic Residues</scene> The hydroxyl chain of Ser-128 conforms in the direction of the active-serine Ser-81, and contributes to the catalytic mechanism.<ref name="Santillana" />
 == Hydrolysis Mechanism ==