1jll

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1jll

Crystal Structure Analysis of the E197betaA Mutant of E. coli SCS

Authors Fraser, M.E. Joyce, M.A. Ryan, D.G. Wolodko, W.T.
Citation Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase. PubMed
Release date 2002-01-30
Exp. Method X-RAY DIFFRACTION
Resolution 2.69 Å
Classification LIGASE

Sequence

Chain A (288 residues): Blast Uniprot
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDS
ILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEA
VKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPK
GKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK
Chain B (388 residues): Blast Uniprot EC 6.2.1.5
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR
LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG
RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIAINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP
REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG
GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK
Chain D (288 residues): Blast Uniprot
SILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDS
ILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEA
VKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPK
GKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK
Chain E (388 residues): Blast Uniprot EC 6.2.1.5
MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR
LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG
RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIAINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP
REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG
GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK


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