Replication Termination Protein

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<scene name='Rtp_and_Tus_DNA_Binding/Wingdown/1'>Wing-down</scene>: Contacts with phosphate backbone of downstream DNA
<scene name='Rtp_and_Tus_DNA_Binding/Wingdown/1'>Wing-down</scene>: Contacts with phosphate backbone of downstream DNA
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<Structure load='Lol1.pdb' size='400' color='white'/>
<scene name='Replication_Termination_Protein/Binding/1'>Residues binding to DNA</scene>
<scene name='Replication_Termination_Protein/Binding/1'>Residues binding to DNA</scene>
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Residues binding in both RTP monomers: Gln15, Arg16, Leu35, Asn53, His54, Thr55, Tyr58, Arg59, His62, gln72 (RED)
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Residues that bind in both monomers: Red
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Residues binding in only wing down position: Lys14, Tyr33, Lys77, Gln83, Val86 (BLUE)
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Residues binding in only wing up position: Thr9, Lys36, Glu56 (GREEN)
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-
<Structure load='Lol1.pdb' size='400' color='white'/>
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Residues that bind only in wing-up: Green
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Residues that bind only in wing-down: Blue
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{| class="wikitable"
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|-
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! Both monomers
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! Unit
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! Binding
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|-
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| Lys14
 +
| Wing-down
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| Phosphate(13)
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|-
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| Gln15
 +
| Both
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| Phosphate(14)
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|-
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| Arg16
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| Both
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| Phosphate(13)
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|-
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| Tyr33
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| Wing-down
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| Phosphate(3)
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|-
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| Leu35
 +
| both
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| Phosphate(4)
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|-
 +
| Lys36
 +
| Wing-up
 +
| Sugar(3)
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|-
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| Asn53
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| Both
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| Phosphate(14)
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|-
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| His54
 +
| Both
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| Guanine(5)
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|-
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| Thr55
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| Both
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| Thymine(15)
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|-
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| Glu56
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| Wing-up
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| Phosphate(13)
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|-
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| Tyr58
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| Both
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| Phosphate(4/5)
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|-
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| Arg59
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| Both
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| Guanine(14)
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|-
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| His62
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| Both
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| Phosphate(5)
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|-
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| Gln72
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| Both
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| Phosphate(5)
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|-
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| Lys77
 +
| Wing-down
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| Phosphate(3)
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|-
 +
| Gln83
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| Wing-down
 +
| Sugar(3)
 +
|-
 +
| Val86
 +
| Wind-down
 +
| Phosphate(4)
 +
|-
 +
|}

Revision as of 04:35, 23 May 2011

Replication Termination Proteins

Rtp and Tus These polar fork bocking sites have been found in yeast, pea, frog and human genomes.

RTP

RTP is a DNA binding protein from Bacillus Subtilis that uses a helix-loop-helix binding motif. In solution it shows a symmetric structure typical of the winged helix loop helix family, with an unstructured end, first alpha helix , unstructured loop that is equivalent to the first beta sheet , helix loop helix structure (-), 2 beta sheets with a connecting loop that makes up the 'wing' structure and an additional long alpha helix involved in dimerisation .

Assymmetry of RTP in DNA-binding

: Contacts upstream with rtp dimer bound to A-site

: Contacts with phosphate backbone of downstream DNA

Drag the structure with the mouse to rotate


Residues that bind in both monomers: Red

Residues that bind only in wing-up: Green

Residues that bind only in wing-down: Blue

Both monomers Unit Binding
Lys14 Wing-down Phosphate(13)
Gln15 Both Phosphate(14)
Arg16 Both Phosphate(13)
Tyr33 Wing-down Phosphate(3)
Leu35 both Phosphate(4)
Lys36 Wing-up Sugar(3)
Asn53 Both Phosphate(14)
His54 Both Guanine(5)
Thr55 Both Thymine(15)
Glu56 Wing-up Phosphate(13)
Tyr58 Both Phosphate(4/5)
Arg59 Both Guanine(14)
His62 Both Phosphate(5)
Gln72 Both Phosphate(5)
Lys77 Wing-down Phosphate(3)
Gln83 Wing-down Sugar(3)
Val86 Wind-down Phosphate(4)

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Craig Mooney, Joel L. Sussman

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