Serine hydroxymethyltransferase: Difference between revisions
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[[Image:RibbonDiagramSHMT.png|thumb|right|200px| Ribbon Diagram of bsSHMT with bound PLP]] | [[Image:RibbonDiagramSHMT.png|thumb|right|200px| Ribbon Diagram of bsSHMT with bound PLP]] | ||
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=Structure and Folding= | =Structure and Folding= | ||
Serine Hydroxymethyltransferase exists in different forms. In "Bacillus Stearthermophilus", SHMT exists as a dimer with two monomeric folds comprised of two separate domains. The enzyme monomer fold is comprised of the C-terminal domain and the N-Terminal Domain. The C-terminal domain folds into an αβ sandwich. The N-terminal domain is comprised of two further sub-domains. The first N-terminal sub-domain is a smaller domain composed of only 3 α-helices and 1 β-strand. The second N-terminal subdomain is the PLP binding domain. This sub-domain folds into an αβα structure that has a seven-stranded mixed β sheet surrounded by α-helices on both sides, hence αβα. Thus far, only X-Ray crystallography has been utilized in the determination of SHMT structure. Successful X-Ray crystals have been developed for the protein alone and for protein in the presence of substrate. These crystal structures, however, mostly consist of SHMT parts pieced together through various studies. A whole 3D structure for one specific organism has yet to be crystallized. As a result of the lack of a pure 3D structure, forming a SHMT crystal structure with inhibitor present has been unsuccessful. | Serine Hydroxymethyltransferase exists in different forms. In "Bacillus Stearthermophilus", SHMT exists as a dimer with two monomeric folds comprised of two separate domains. The enzyme monomer fold is comprised of the C-terminal domain and the N-Terminal Domain. The C-terminal domain folds into an αβ sandwich. The N-terminal domain is comprised of two further sub-domains. The first N-terminal sub-domain is a smaller domain composed of only 3 α-helices and 1 β-strand. The second N-terminal subdomain is the PLP binding domain. This sub-domain folds into an αβα structure that has a seven-stranded mixed β sheet surrounded by α-helices on both sides, hence αβα. Thus far, only X-Ray crystallography has been utilized in the determination of SHMT structure. Successful X-Ray crystals have been developed for the protein alone and for protein in the presence of substrate. These crystal structures, however, mostly consist of SHMT parts pieced together through various studies. A whole 3D structure for one specific organism has yet to be crystallized. As a result of the lack of a pure 3D structure, forming a SHMT crystal structure with inhibitor present has been unsuccessful. | ||