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.


1r48

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r48.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1r48.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r48| PDB=1r48 | SCENE= }}
{{STRUCTURE_1r48| PDB=1r48 | SCENE= }}
-
'''Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP'''
+
===Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP===
-
==Overview==
+
<!--
-
Bacteria respond to increasing medium osmolality by accumulating organic solutes that are compatible with cellular functions. Transporter ProP of Escherichia coli, a proton symporter and a member of the major facilitator superfamily, senses osmotic shifts and responds by importing osmolytes such as glycine betaine. ProP contains a cytoplasmic, C-terminal extension that is essential for its activity. A peptide corresponding to the C-terminal extension of ProP forms a homodimeric alpha-helical coiled-coil even though some of its heptad a positions are not occupied by hydrophobic amino acid residues. Unexpectedly, amino acid replacement R488I, occurring at a heptad a position, destabilized the coiled-coil formed by the ProP peptide and attenuated the response of the intact transporter to osmotic upshifts in vivo. Thus, ProP was proposed to dimerize via an antiparallel coiled-coil. We used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the synthetic peptide corresponding to residues 468-497 of ProP. This region did form an antiparallel coil-coil in which critical residue R488 specifies the antiparallel coiled-coil orientation by forming stabilizing salt-bridges. Charged residues (both acidic and basic) are clustered on the c/g surface of the coiled-coil whereas polar residues are distributed on the b/e surface. This causes the structure to be bent, in contrast to other known antiparallel coiled-coils (those from the hepatitis delta antigen (PDB ID code 1A92) and the bovine F(1) ATPase inhibitor protein (PDB ID code 1HF9)). The coiled-coil and its possible importance for osmosensing are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14643666}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14643666 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14643666}}
==About this Structure==
==About this Structure==
-
1R48 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA].
+
1R48 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Osmosensor]]
[[Category: Osmosensor]]
[[Category: Two-stranded homodimer]]
[[Category: Two-stranded homodimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:03:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:54:22 2008''

Revision as of 13:54, 27 July 2008

Image:1r48.png

Template:STRUCTURE 1r48

Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP

Template:ABSTRACT PUBMED 14643666

About this Structure

1R48 is a Single protein structure. Full experimental information is available from OCA.

Reference

Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP., Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS, J Mol Biol. 2003 Dec 12;334(5):1063-76. PMID:14643666

Page seeded by OCA on Sun Jul 27 16:54:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r48"
Personal tools