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Loop Conformation and Dynamics of the Escherichia coli HPPK Apo-Enzyme and Its Binary Complex with MgATP
Comparison of the crystallographic and NMR structures of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) suggests that the enzyme may undergo significant conformational change upon binding to its first substrate, ATP. Two of the three surface loops (loop 2 and loop 3) accounting for most...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Biophysical Society
2005
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1366583/ https://ncbi.nlm.nih.gov/pubmed/15821168 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.061556 |
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