1zeq: Difference between revisions

Line 1:

[[Image:1zeq.~~gif~~|left|200px]]

[[Image:1zeq.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli~~'''~~

===1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli===

~~==Overview==~~

<!--

~~We have determined the crystal structure of apo-CusF~~, ~~a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel~~, ~~classified~~ as ~~an OB-fold, which is a unique topology for a copper-binding protein~~. ~~NMR chemical shift mapping experiments suggest that Cu(I~~) is ~~bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of~~ the ~~beta-barrel, and their side chains are oriented toward the interior of the barrel~~. ~~Cu(I) can be modeled into the apo~~-~~CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper~~-~~binding proteins.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16060662}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16060662 is the PubMed ID number.

-->

==About this Structure==

Line 34:

Line 38:

[[Category: Metallochaperone]]

[[Category: Ob-fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 17~~:32:08 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:53:56 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1zeq.gif|left|200px]]
+{{Seed}}
+[[Image:1zeq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1zeq|  PDB=1zeq  |  SCENE=  }}
-'''1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli'''
+===1.5 A Structure of apo-CusF residues 6-88 from Escherichia coli===
-==Overview==
+<!--
-We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of the beta-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_16060662}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16060662 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16060662}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Metallochaperone]]
 [[Category: Ob-fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:32:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:53:56 2008''