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1vqa

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 ==GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)==
-<StructureSection load='1vqa' size='340' side='right' caption='[[1vqa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1vqa' size='340' side='right'caption='[[1vqa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1vqa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpf1 Bpf1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VQA FirstGlance]. <br>
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Bpf1]]
+[[Category: Large Structures]]
 [[Category: Skinner, M M]]
 [[Category: Terwilliger, T C]]

Revision as of 10:10, 8 January 2020

GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)

spinqualitylabelsall models

PDB ID 1vqa

Show:Asymmetric Unit Biological Assembly

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Structural highlights

1vqa is a 1 chain structure with sequence from Bpf1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[G5P_BPF1] Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single-stranded (progeny) viral DNA, prevents the conversion into the double-stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects.

Potential use of additivity of mutational effects in simplifying protein engineering.,Skinner MM, Terwilliger TC Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:8855252^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Skinner MM, Terwilliger TC. Potential use of additivity of mutational effects in simplifying protein engineering. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10753-7. PMID:8855252

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

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1vqa

From Proteopedia

Revision as of 10:10, 8 January 2020

GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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Proteopedia Page Contributors and Editors (what is this?)

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