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ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8
Proteins, structure, function, and bioinformatics, 2005-01, Vol.58 (1), p.235-242
Seto, Azusa
Murayama, Kazutaka
Toyama, Mitsutoshi
Ebihara, Akio
Nakagawa, Noriko
Kuramitsu, Seiki
Shirouzu, Mikako
Yokoyama, Shigeyuki
2005
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Seto, Azusa
Murayama, Kazutaka
Toyama, Mitsutoshi
Ebihara, Akio
Nakagawa, Noriko
Kuramitsu, Seiki
Shirouzu, Mikako
Yokoyama, Shigeyuki
Titel
ATP-induced structural change of dephosphocoenzyme A kinase from Thermus thermophilus HB8
Ist Teil von
Proteins, structure, function, and bioinformatics, 2005-01, Vol.58 (1), p.235-242
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2005
Quelle
Wiley Online Library All Journals
Beschreibungen/Notizen
Dephosphocoenzyme A kinase (DCK) catalyzes phosphorylation in the final step of coenzyme A (CoA) biosynthesis. In this phosphorylation process, domain movements play a very important role. To reveal the structural changes induced by ligand binding, we determined the crystal structure of DCK from Thermus thermophilus HB8 by the multiwavelength anomalous dispersion method at 2.8 Å. The crystal structure includes three independent protein molecules in the asymmetric unit: One is a liganded form and the others are unliganded. The topology shows a canonical nucleotide‐binding protein possessing the P‐loop motif. A structure homology search by DALI revealed the similarity of the DCKs from T. thermophilus HB8, Haemophilus influenzae, and Escherichia coli. Structural comparisons between the liganded and unliganded forms of DCK from T. thermophilus HB8 indicated domain movements induced by adenosine triphosphate (ATP) binding. For the domain movements, proline residues confer flexibility at the domain linkages. In particular, Pro91 plays an important role in moving the CoA domain. Proteins 2005. © 2004 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0887-3585
eISSN: 1097-0134
DOI: 10.1002/prot.20276
Titel-ID: cdi_proquest_miscellaneous_67348024
Format
–
Schlagworte
Adenosine Triphosphate - chemistry
,
Amino Acid Sequence - genetics
,
ATP binding
,
Bacterial Proteins - chemistry
,
Bacterial Proteins - genetics
,
Bacterial Proteins - metabolism
,
Binding Sites - physiology
,
crystal structure
,
Crystallography, X-Ray - methods
,
kinase
,
Ligands
,
Models, Molecular
,
Molecular Sequence Data
,
Phosphotransferases (Alcohol Group Acceptor) - chemistry
,
Phosphotransferases (Alcohol Group Acceptor) - genetics
,
Phosphotransferases (Alcohol Group Acceptor) - metabolism
,
Protein Structure, Secondary - genetics
,
structural change
,
Thermus thermophilus - chemistry
,
Thermus thermophilus - enzymology
,
Thermus thermophilus - genetics
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