This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2b22

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:46, 16 May 2018

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat

Structural highlights

2b22 is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2zta, 1gcm, 1gcl, 2b1f
Gene:	GCN4, AAS3, ARG9 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.

Publication Abstract from PubMed

Coiled-coil sequences in proteins commonly share a seven-amino acid repeat with nonpolar side chains at the first (a) and fourth (d) positions. We investigate here the role of a 3-3-1 hydrophobic repeat containing nonpolar amino acids at the a, d, and g positions in determining the structures of coiled coils using mutants of the GCN4 leucine zipper dimerization domain. When three charged residues at the g positions in the parental sequence are replaced by nonpolar alanine or valine side chains, stable four-helix structures result. The X-ray crystal structures of the tetramers reveal antiparallel, four-stranded coiled coils in which the a, d, and g side chains interlock in a combination of knobs-into-knobs and knobs-into-holes packing. Interfacial interactions in a coiled coil can therefore be prescribed by hydrophobic-polar patterns beyond the canonical 3-4 heptad repeat. The results suggest that the conserved, charged residues at the g positions in the GCN4 leucine zipper can impart a negative design element to disfavor thermodynamically more stable, antiparallel tetramers.

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat.,Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M Structure. 2006 Feb;14(2):247-55. PMID:16472744^[1]

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

References

↑ Deng Y, Liu J, Zheng Q, Eliezer D, Kallenbach NR, Lu M. Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat. Structure. 2006 Feb;14(2):247-55. PMID:16472744 doi:S0969-2126(06)00046-3

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b22"

@@ Line 1: / Line 1: @@
 ==Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat==
 <StructureSection load='2b22' size='340' side='right' caption='[[2b22]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zta|2zta]], [[1gcm|1gcm]], [[1gcl|1gcl]], [[2b1f|2b1f]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GCN4, AAS3, ARG9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b22 OCA], [http://pdbe.org/2b22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b22 RCSB], [http://www.ebi.ac.uk/pdbsum/2b22 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b22 OCA], [http://pdbe.org/2b22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b22 RCSB], [http://www.ebi.ac.uk/pdbsum/2b22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b22 ProSAT]</span></td></tr>
 </table>
 == Function ==

2b22

From Proteopedia

Revision as of 06:46, 16 May 2018

Antiparallel four-stranded coiled coil specified by a 3-3-1 hydrophobic heptad repeat

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox