Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism
المؤلفون المشاركون
Li, Yixue
Ping, Jie
Wang, Jing-Fang
Hao, Pei
المصدر
العدد
المجلد 2013، العدد 2013 (31 ديسمبر/كانون الأول 2013)، ص ص. 1-7، 7ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2013-06-26
دولة النشر
مصر
عدد الصفحات
7
التخصصات الرئيسية
الملخص EN
Escherichia coli adenylate kinase (ADK) is a monomeric phosphotransferase enzyme that catalyzes reversible transfer of phosphoryl group from ATP to AMP with a large-scale domain motion.
The detailed mechanism for this conformational transition remains unknown.
In the current study, we performed long time-scale molecular dynamics simulations on both open and closed states of ADK.
Based on the structural analyses of the simulation trajectories, we detected over 20 times conformational transitions between the open and closed states of ADK and identified two novel conformations as intermediate states in the catalytic processes.
With these findings, we proposed a possible mechanism for the large-scale domain motion of Escherichia coli ADK and its catalytic process: (1) the substrate free ADK adopted an open conformation; (2) ATP bound with LID domain closure; (3) AMP bound with NMP domain closure; (4) phosphoryl transfer occurred with ATP, and AMP converted into two ADPs, and no conformational transition was detected in the enzyme; (5) LID domain opened with one ADP released; (6) another ADP released with NMP domain open.
As both open and closed states sampled a wide range of conformation transitions, our simulation strongly supported the conformational selection mechanism for Escherichia coli ADK.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
Ping, Jie& Hao, Pei& Li, Yixue& Wang, Jing-Fang. 2013. Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism. BioMed Research International،Vol. 2013, no. 2013, pp.1-7.
https://search.emarefa.net/detail/BIM-1004760
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
Ping, Jie…[et al.]. Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism. BioMed Research International No. 2013 (2013), pp.1-7.
https://search.emarefa.net/detail/BIM-1004760
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
Ping, Jie& Hao, Pei& Li, Yixue& Wang, Jing-Fang. Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-7.
https://search.emarefa.net/detail/BIM-1004760
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1004760
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
تقوم هذه الخدمة بالتحقق من التشابه أو الانتحال في الأبحاث والمقالات العلمية والأطروحات الجامعية والكتب والأبحاث باللغة العربية، وتحديد درجة التشابه أو أصالة الأعمال البحثية وحماية ملكيتها الفكرية. تعرف اكثر