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| | {{STRUCTURE_1np6| PDB=1np6 | SCENE= }} | | {{STRUCTURE_1np6| PDB=1np6 | SCENE= }} |
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| - | '''Crystal structure of Escherichia coli MobB'''
| + | ===Crystal structure of Escherichia coli MobB=== |
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| - | ==Overview==
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| - | Two proteins, which are co-transcribed in Escherichia coli (MobA and MobB), are involved in the attachment of a nucleotide moiety to the molybdenum cofactor to form active molybdopterin guanine dinucleotide. Although not essential for this process, the dimeric MobB increases the activation of molybdoenzymes, incorporating this cofactor by a mechanism that is not understood. The structure of MobB has been elucidated in two crystal forms, one of which has provided a model at 1.9-A resolution with Rwork and Rfree values of 21.5 and 28.7%, respectively. The MobB subunit displays an alpha/beta-fold arranged into a major and minor domain, the latter of which is inserted between the major and minor domains of the partner subunit, creating an elongated dimer constructed around a 16-stranded beta-sheet. Structural homologues have been identified, and they include a number of nucleotide-binding proteins. Comparisons indicate that although the phosphate-binding regions are highly conserved, MobB lacks the elements of structure required to interact with and efficiently bind a nucleotide base. In the present structure, a sulfate is bound to the Walker A phosphate-binding motif of MobB. The possibility that MobB forms a complex with the nucleotide-binding MobA, the protein with which it is co-transcribed, is explored, and modeling suggests that such a MobA:MobB complex is feasible. This hypothesis is supported by recent biochemical evidence indicating that MobB interacts with several proteins involved in various stages of molybdenum cofactor biosynthesis including MobA. We propose therefore that MobB is an adapter protein that acts in concert with MobA to achieve the efficient biosynthesis and utilization of molybdopterin guanine dinucleotide.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12682065}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12682065 is the PubMed ID number. |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: P-loop structural motif]] | | [[Category: P-loop structural motif]] |
| | [[Category: Walker a motif]] | | [[Category: Walker a motif]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:48:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:02:59 2008'' |
Revision as of 12:03, 29 July 2008
Template:STRUCTURE 1np6
Crystal structure of Escherichia coli MobB
Template:ABSTRACT PUBMED 12682065
About this Structure
1NP6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure., McLuskey K, Harrison JA, Schuttelkopf AW, Boxer DH, Hunter WN, J Biol Chem. 2003 Jun 27;278(26):23706-13. Epub 2003 Apr 7. PMID:12682065
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