1h9m
From Proteopedia
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| - | [[Image:1h9m.jpg|left|200px]] | + | [[Image:1h9m.jpg|left|200px]] |
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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. PEG-GROWN FORM WITH MOLYBDATE BOUND''' | + | {{Structure |
| + | |PDB= 1h9m |SIZE=350|CAPTION= <scene name='initialview01'>1h9m</scene>, resolution 1.65Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Moo+Binding+Site+For+Chain+A1142+Symmetry+Related+Subuni+...'>AC1</scene>, <scene name='pdbsite=AC2:Moo+Binding+Site+For+Chain+A1143+Symmetry+Related+Subuni+...'>AC2</scene>, <scene name='pdbsite=AC3:Moo+Binding+Site+For+Chain+A1144+Symmetry+Related+Subuni+...'>AC3</scene>, <scene name='pdbsite=AC4:Moo+Binding+Site+For+Chain+A1145+Symmetry+Related+Subuni+...'>AC4</scene>, <scene name='pdbsite=AC5:Moo+Binding+Site+For+Chain+B1142+Symmetry+Related+Subuni+...'>AC5</scene>, <scene name='pdbsite=AC6:Moo+Binding+Site+For+Chain+B1143+Symmetry+Related+Subuni+...'>AC6</scene>, <scene name='pdbsite=AC7:Moo+Binding+Site+For+Chain+B1144+Symmetry+Related+Subuni+...'>AC7</scene> and <scene name='pdbsite=AC8:Moo+Binding+Site+For+Chain+B1145+Symmetry+Related+Subuni+...'>AC8</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MOO:MOLYBDATE ION'>MOO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= MODG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii]) | ||
| + | }} | ||
| + | |||
| + | '''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''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H9M is a [ | + | 1H9M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H9M OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11352591 11352591] |
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: molybdate homeostasis]] | [[Category: molybdate homeostasis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:08 2008'' |
Revision as of 09:34, 20 March 2008
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| , resolution 1.65Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | MODG (Azotobacter vinelandii) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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
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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