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.


1fr3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fr3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fr3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fr3| PDB=1fr3 | SCENE= }}
{{STRUCTURE_1fr3| PDB=1fr3 | SCENE= }}
-
'''THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA'''
+
===THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA===
-
==Overview==
+
<!--
-
BACKGROUND: Transport of molybdenum into bacteria involves a high-affinity ABC transporter system whose expression is controlled by a repressor protein called ModE. While molybdate transport is tightly coupled to utilization in some bacteria, other organisms have molybdenum storage proteins. One class of putative molybdate storage proteins is characterized by a sequence consisting of about 70 amino acids (Mop). A tandem repeat of Mop sequences also constitutes the molybdate binding domain of ModE. RESULTS: We have determined the crystal structure of the 7 kDa Mop protein from the methanol-utilizing anaerobic eubacterium Sporomusa ovata grown in the presence of molybdate and tungstate. The protein occurs as highly symmetric hexamers binding eight oxyanions. Each peptide assumes a so-called OB fold, which has previously also been observed in ModE. There are two types of oxyanion binding sites in Mo at the interface between two or three peptides. All oxyanion binding sites were found to be occupied by WO(4) rather than MoO(4). CONCLUSIONS: The biological function of proteins containing only Mop sequences is unknown, but they have been implicated in molybdate homeostasis and molybdopterin cofactor biosynthesis. While there are few indications that the S. ovata Mop binds pterin, the structure suggests that only the type-1 oxyanion binding sites would be sufficiently accessible to bind a cofactor. The observed occupation of the oxyanion binding sites by WO(4) indicates that Mop might also be involved in controlling intracellular tungstate levels.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11080635}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11080635 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11080635}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Molybdate homeostasis]]
[[Category: Molybdate homeostasis]]
[[Category: Tungstate]]
[[Category: Tungstate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:40:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:49:00 2008''

Revision as of 00:49, 1 July 2008

Image:1fr3.png

Template:STRUCTURE 1fr3

THE HIGH RESOLUTION STRUCTURE OF A MOLYBDATE BINDING PROTEIN FROM SPOROMUSA OVATA

Template:ABSTRACT PUBMED 11080635

About this Structure

1FR3 is a Single protein structure of sequence from Sporomusa ovata. Full crystallographic information is available from OCA.

Reference

Structure of the molybdate/tungstate binding protein mop from Sporomusa ovata., Wagner UG, Stupperich E, Kratky C, Structure. 2000 Nov 15;8(11):1127-36. PMID:11080635

Page seeded by OCA on Tue Jul 1 03:49:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fr3"
Personal tools