1qx8

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{{STRUCTURE_1qx8| PDB=1qx8 | SCENE= }}
{{STRUCTURE_1qx8| PDB=1qx8 | SCENE= }}
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'''Crystal structure of a five-residue deletion mutant of the Rop protein'''
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===Crystal structure of a five-residue deletion mutant of the Rop protein===
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==Overview==
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The repressor of primer (Rop) protein has become a steady source of surprises concerning the relationship between the sequences and the structures of several of its mutants and variants. Here we add another piece to the puzzle of Rop by showing that an engineered deletion mutant of the protein (corresponding to a deletion of residues 30-34 of the wild-type protein and designed to restore the heptad periodicity at the turn region) results in a complete reorganization of the bundle which is converted from a homodimer to a homotetramer. In contrast (and as previously shown), a two-residue insertion, which also restores the heptad periodicity, is essentially identical with wild-type Rop. The new deletion mutant structure is a canonical, left-handed, all-antiparallel bundle with a completely different hydrophobic core and distinct surface properties. The structure agrees and qualitatively explains the results from functional, thermodynamic, and kinetic studies which indicated that this deletion mutant is a biologically inactive hyperstable homotetramer. Additional insight into the stability and dynamics of the mutant structure has been obtained from extensive molecular dynamics simulations in explicit water and with full treatment of electrostatics.
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The line below this paragraph, {{ABSTRACT_PUBMED_16953576}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16953576 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16953576}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein., Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M, Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16953576 16953576]
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein., Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M, Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16953576 16953576]
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Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants., Papanikolau Y, Kotsifaki D, Fadouloglou VE, Gazi AD, Glykos NM, Cesareni G, Kokkinidis M, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1334-7. Epub 2004, Jun 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15213408 15213408]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rna primer]]
[[Category: Rna primer]]
[[Category: X-ray]]
[[Category: X-ray]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:48:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:53:37 2008''

Revision as of 04:53, 28 July 2008

Image:1qx8.png

Template:STRUCTURE 1qx8

Crystal structure of a five-residue deletion mutant of the Rop protein

Template:ABSTRACT PUBMED 16953576

About this Structure

1QX8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein., Glykos NM, Papanikolau Y, Vlassi M, Kotsifaki D, Cesareni G, Kokkinidis M, Biochemistry. 2006 Sep 12;45(36):10905-19. PMID:16953576

Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants., Papanikolau Y, Kotsifaki D, Fadouloglou VE, Gazi AD, Glykos NM, Cesareni G, Kokkinidis M, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1334-7. Epub 2004, Jun 22. PMID:15213408

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