Stirrup protein domain: Difference between revisions
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In [[molecular biology]], the [[protein domain]] '''Stirrup''' is a domain, found only in found in [[domain (biology)|domain]], [[archaea]]. The Stirrup protein domain is found in [[prokaryotic]] [[protein]] [[ribonucleotide]] reductases. It obtains its name due to its resemblance to |
In [[molecular biology]], the [[protein domain]] '''Stirrup''' is a domain, found only in found in the [[domain (biology)|domain]], [[archaea]]. The Stirrup protein domain is found in [[prokaryotic]] [[protein]] [[ribonucleotide]] [[Reductase|reductases]]. It obtains its name due to its resemblance to an old fashioned [[Abumi (stirrup)|Japanese stirrup]]. Stirrip has a [[molecular mass]] of 9 kDa and is [[protein folding|folded]] into an alpha/beta [[secondary structure|structure]]. It allows for [[Binding (molecular)|binding]] of the [[reductase]] to DNA via [[electrostatic]] interactions, since it has a predominance of [[positive predictive value|positive]] charges distributed on its surface.<ref name="pmid10891276">{{cite journal | vauthors = Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K | title = Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI | journal = Journal of Molecular Biology | volume = 300 | issue = 4 | pages = 889–901 | date = July 2000 | pmid = 10891276 | doi = 10.1006/jmbi.2000.3873 }}</ref> |
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==Function== |
== Function == |
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This protein domain provides the [[ |
This protein domain provides the [[precursor (chemistry)|precursor]]s necessary for [[DNA]] synthesis. It catalyses the [[biosynthesis]] of [[DNA]] from [[RNA]].<ref>{{cite web|url=https://www.uniprot.org/uniprot/P95484|title=Ribonucleoside-diphosphate reductase|work=UniProt|access-date=14 August 2012}}</ref> |
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==Structure== |
== Structure == |
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This structure contains a three-stranded [[beta-sheet]] to the solvent, which lies against [[alpha helix|alpha-helices]]<ref name="pmid10891276"/> |
This structure contains a three-stranded [[beta-sheet]] to the solvent, which lies against [[alpha helix|alpha-helices]].<ref name="pmid10891276"/> |
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==References== |
== References == |
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{{reflist}} |
{{reflist}} |
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{{InterPro content|IPR015146}} |
{{InterPro content|IPR015146}} |
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[[Category:Protein domains]] |
[[Category:Protein domains]] |
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[[Category:Archaea]] |
[[Category:Archaea biology]] |
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[[Category:Protein families]] |
[[Category:Protein families]] |
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Latest revision as of 17:24, 29 August 2024
| Stirrup | |||||||||
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 crystal structure of an archaeal intein-encoded homing endonuclease pi-pfui | |||||||||
| Identifiers | |||||||||
| Symbol | Stirrup | ||||||||
| Pfam | PF09061 | ||||||||
| InterPro | IPR015146 | ||||||||
| SCOP2 | 1dq3 / SCOPe / SUPFAM | ||||||||
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In molecular biology, the protein domain Stirrup is a domain, found only in found in the domain, archaea. The Stirrup protein domain is found in prokaryotic protein ribonucleotide reductases. It obtains its name due to its resemblance to an old fashioned Japanese stirrup. Stirrip has a molecular mass of 9 kDa and is folded into an alpha/beta structure. It allows for binding of the reductase to DNA via electrostatic interactions, since it has a predominance of positive charges distributed on its surface.[1]
Function
[edit]This protein domain provides the precursors necessary for DNA synthesis. It catalyses the biosynthesis of DNA from RNA.[2]
Structure
[edit]This structure contains a three-stranded beta-sheet to the solvent, which lies against alpha-helices.[1]
References
[edit]- ^ a b Ichiyanagi K, Ishino Y, Ariyoshi M, Komori K, Morikawa K (July 2000). "Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI". Journal of Molecular Biology. 300 (4): 889–901. doi:10.1006/jmbi.2000.3873. PMID 10891276.
- ^ "Ribonucleoside-diphosphate reductase". UniProt. Retrieved 14 August 2012.