1h9k
From Proteopedia
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| - | [[Image:1h9k.jpg|left|200px]]<br /><applet load="1h9k" size=" | + | [[Image:1h9k.jpg|left|200px]]<br /><applet load="1h9k" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h9k, resolution 1.80Å" /> | caption="1h9k, resolution 1.80Å" /> | ||
'''TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PHOSPHATE-GROWN FORM WITH TUNGSTATE AND PHOSPHATE BOUND'''<br /> | '''TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PHOSPHATE-GROWN FORM WITH TUNGSTATE AND PHOSPHATE BOUND'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with WO4 and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=WO1:Wo4 Binding Site For Chain A Symmetry Related Subunits C ...'>WO1</scene> and <scene name='pdbsite=WO2:Wo4 Binding Site For Chain A Symmetry Related Subunits C ...'>WO2</scene>. Full crystallographic information is available from [http:// | + | 1H9K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=WO4:'>WO4</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=WO1:Wo4+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>WO1</scene> and <scene name='pdbsite=WO2:Wo4+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>WO2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: molybdate homeostasis]] | [[Category: molybdate homeostasis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:59 2008'' |
Revision as of 07:47, 3 February 2008
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TWO CRYSTAL STRUCTURES OF THE CYTOPLASMIC MOLYBDATE-BINDING PROTEIN MODG SUGGEST A NOVEL COOPERATIVE BINDING MECHANISM AND PROVIDE INSIGHTS INTO LIGAND-BINDING SPECIFICITY. PHOSPHATE-GROWN FORM WITH TUNGSTATE AND PHOSPHATE BOUND
Overview
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.
About this Structure
1H9K is a Single protein structure of sequence from Azotobacter vinelandii with and as ligands. Known structural/functional Sites: and . 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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