Sandbox Reserved 1094: Difference between revisions
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This sequence being the normal protein sequence found in L. ''mesenteroides''. | This sequence being the normal protein sequence found in L. ''mesenteroides''. | ||
== Structural highlights == | == Structural highlights == | ||
Glucose-6-Phosphate Dehydrogenase is formed of a homodimer, so a dimer of two identical [https://en.wikipedia.org/wiki/Protein_subunit subunit]. | |||
'''Secondary structure''' | |||
A subunit contains 485 residues where 285 residues are in secondary structure. 93 residues are involved in 15 β-sheet strands and 192 in 17 helices. | |||
'''Tertiary structure''' | |||
Each <scene name='82/829347/Monomerg6pd/1'>monomer</scene> is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/5'>1 red and 1 green</scene>. | |||
Depending on several conditions, it can dimerize to form tetramers. Each monomer is composed of a small domain localized in the amino terminal part which constitute the coenzyme binding domain and a larger domain in the carboxy terminal part which constitute the substrate binding domain. the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+ using the Rossman fold.<ref name="struc">PMID: 7881907</ref> | |||
