1h9m: Difference between revisions

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[[Image:1h9m.jpg|left|200px]]
{{Seed}}
[[Image:1h9m.png|left|200px]]


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{{STRUCTURE_1h9m|  PDB=1h9m  |  SCENE=  }}  
{{STRUCTURE_1h9m|  PDB=1h9m  |  SCENE=  }}  


'''TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PEG-GROWN FORM WITH MOLYBDATE BOUND'''
===TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PEG-GROWN FORM WITH MOLYBDATE BOUND===




==Overview==
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The X-ray structures of the cytoplasmic molybdate-binding protein ModG from Azotobacter vinelandii in two different crystal forms have been determined. For such a small protein it is remarkably complex. Each 14.3 kDa subunit contains two small beta-barrel domains, which display an OB-fold motif, also seen in the related structure of ModE, a molybdenum-dependent transcriptional regulator, and very recently in the Mop protein that, like ModG, has been implicated in molybdenum homeostasis within the cell. In contrast to earlier speculation, the functional unit of ModG is actually not a dimer (as in ModE), but a trimer capable of binding a total of eight molybdate molecules that are distributed between two disparate types of site. All the binding sites are located at subunit interfaces, with one type lying on a crystallographic 3-fold axis, whilst the other lies between pairs of subunits. The two types of site are linked by short hydrogen bond networks that may suggest a cooperative binding mechanism. A superposition of two subunits of the ModG trimer on the apo-ModE dimer allows the probable locations of the molybdate-binding sites of the latter to be assigned. Through structural comparisons with other oxyanion-binding proteins, including Mop and ModE, it is possible to speculate about ligand-binding affinities, selectivity and evolution. Copyright 12001 Academic Press.
The line below this paragraph, {{ABSTRACT_PUBMED_11352591}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11352591 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11352591}}


==About this Structure==
==About this Structure==
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[[Category: Binding protein]]
[[Category: Binding protein]]
[[Category: Molybdate homeostasis]]
[[Category: Molybdate homeostasis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:36:37 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:51:19 2008''

Revision as of 04:51, 1 July 2008

File:1h9m.png

Template:STRUCTURE 1h9m

TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PEG-GROWN FORM WITH MOLYBDATE BOUND

Template:ABSTRACT PUBMED 11352591

About this Structure

1H9M is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.

Reference

Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity., Delarbre L, Stevenson CE, White DJ, Mitchenall LA, Pau RN, Lawson DM, J Mol Biol. 2001 May 18;308(5):1063-79. PMID:11352591

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