Structure of the carboxypeptidase t from Thermoactinomyces vulgaris complex with L - phenyl lactate

Мұқаба

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат Ашық рұқсат
Рұқсат жабық Рұқсат берілді
Рұқсат жабық Тек жазылушылар үшін

Аннотация

The crystal structure of the metallocarboxypeptidase T from Thermoactinomyces vulgaris complex with L-phenylactate was obtained with a resolution of 1.73 Å. Unlike pancreatic carboxypeptidase A, which binds one L-phenylactate molecule, in complex with CPT, the ligand occupies both S1 and S1ʹ sites of the active center simultaneously. In this case, conformational changes occur that differ from the changes caused by the alternate occupation of the S1 and S1ʹ sites by BOC-leucine and benzylsuccinic acid. These changes concern the residues E277, E59, L254, G192, S127 and Y218 and reach a span of 0.77 Å. A conclusion is made about the possible role of these residues in the recognition and catalysis of substrates by carboxypeptidase T.

Толық мәтін

Рұқсат жабық

Авторлар туралы

V. Akparov

Shubnikov Institute of Crystallography of Kurchatov Complex of Crystallography and Photonics of NRC “Kurchatov Institute”

Хат алмасуға жауапты Автор.
Email: valery.akparov@yandex.ru
Ресей, Moscow

G. Konstantinova

Shubnikov Institute of Crystallography of Kurchatov Complex of Crystallography and Photonics of NRC “Kurchatov Institute”

Email: valery.akparov@yandex.ru
Ресей, Moscow

V. Timofeev

Shubnikov Institute of Crystallography of Kurchatov Complex of Crystallography and Photonics of NRC “Kurchatov Institute”

Email: valery.akparov@yandex.ru
Ресей, Moscow

M. Shvetsov

Moscow Institute of Physics and Technology

Email: valery.akparov@yandex.ru
Ресей, Dolgoprudny

I. Kuranova

Shubnikov Institute of Crystallography of Kurchatov Complex of Crystallography and Photonics of NRC “Kurchatov Institute”; Moscow Institute of Physics and Technology

Email: valery.akparov@yandex.ru
Ресей, Moscow; Dolgoprudny

Әдебиет тізімі

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