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.


1ykg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ykg.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ykg.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ykg| PDB=1ykg | SCENE= }}
{{STRUCTURE_1ykg| PDB=1ykg | SCENE= }}
-
'''Solution structure of the flavodoxin-like domain from the Escherichia coli sulfite reductase'''
+
===Solution structure of the flavodoxin-like domain from the Escherichia coli sulfite reductase===
-
==Overview==
+
<!--
-
The flavoprotein moiety of Escherichia coli sulfite reductase (SiR-FP) is homologous to electron transfer proteins such as cytochrome-P450 reductase (CPR) or nitric oxide synthase (NOS). We report on the three-dimensional structure of SiR-FP18, the flavodoxin-like domain of SiR-FP, which has been determined by NMR. In the holoenzyme, this domain plays an important role by shuttling electrons from the FAD to the hemoprotein (the beta-subunit). The structure presented here was determined using distance and torsion angle information in combination with residual dipolar couplings determined in two different alignment media. Several protein-FMN NOEs allowed us to place the prosthetic group in its binding pocket. The structure is well-resolved, and (15)N relaxation data indicate that SiR-FP18 is a compact domain. The binding interface with cytochrome c, a nonphysiological electron acceptor, has been determined using chemical shift mapping. Comparison of the SiR-FP18 structure with the corresponding domains from CPR and NOS shows that the fold of the protein core is highly conserved, but the analysis of the electrostatic surfaces reveals significant differences between the three domains. These observations are placed in the physiological context so they can contribute to the understanding of the electron transfer mechanism in the SiR holoenzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15966732}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15966732 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15966732}}
==About this Structure==
==About this Structure==
-
1YKG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKG OCA].
+
1YKG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKG OCA].
==Reference==
==Reference==
Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli., Sibille N, Blackledge M, Brutscher B, Coves J, Bersch B, Biochemistry. 2005 Jun 28;44(25):9086-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15966732 15966732]
Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli., Sibille N, Blackledge M, Brutscher B, Coves J, Bersch B, Biochemistry. 2005 Jun 28;44(25):9086-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15966732 15966732]
 +
 +
Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain., Champier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J, Biochemistry. 2002 Mar 19;41(11):3770-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11888295 11888295]
 +
 +
1H, 13C and 15N assignment of the flavodoxin-like domain of the Escherichia coli sulfite reductase., Sibille N, Coves J, Marion D, Brutscher B, Bersch B, J Biomol NMR. 2001 Sep;21(1):71-2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11693572 11693572]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 29: Line 37:
[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Flavoprotein]]
[[Category: Flavoprotein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:26:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:54:44 2008''

Revision as of 05:54, 28 July 2008

Image:1ykg.png

Template:STRUCTURE 1ykg

Solution structure of the flavodoxin-like domain from the Escherichia coli sulfite reductase

Template:ABSTRACT PUBMED 15966732

About this Structure

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

Reference

Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli., Sibille N, Blackledge M, Brutscher B, Coves J, Bersch B, Biochemistry. 2005 Jun 28;44(25):9086-95. PMID:15966732

Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain., Champier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J, Biochemistry. 2002 Mar 19;41(11):3770-80. PMID:11888295

1H, 13C and 15N assignment of the flavodoxin-like domain of the Escherichia coli sulfite reductase., Sibille N, Coves J, Marion D, Brutscher B, Bersch B, J Biomol NMR. 2001 Sep;21(1):71-2. PMID:11693572

Page seeded by OCA on Mon Jul 28 08:54:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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