2vee
From Proteopedia
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|PDB= 2vee |SIZE=350|CAPTION= <scene name='initialview01'>2vee</scene>, resolution 2.60Å | |PDB= 2vee |SIZE=350|CAPTION= <scene name='initialview01'>2vee</scene>, resolution 2.60Å | ||
|SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Hem+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Hem+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Hem+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Hem+Binding+Site+For+Chain+E'>AC5</scene>, <scene name='pdbsite=AC6:Hem+Binding+Site+For+Chain+F'>AC6</scene>, <scene name='pdbsite=AC7:Hem+Binding+Site+For+Chain+G'>AC7</scene> and <scene name='pdbsite=AC8:Hem+Binding+Site+For+Chain+H'>AC8</scene> | |SITE= <scene name='pdbsite=AC1:Hem+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Hem+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Hem+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Hem+Binding+Site+For+Chain+D'>AC4</scene>, <scene name='pdbsite=AC5:Hem+Binding+Site+For+Chain+E'>AC5</scene>, <scene name='pdbsite=AC6:Hem+Binding+Site+For+Chain+F'>AC6</scene>, <scene name='pdbsite=AC7:Hem+Binding+Site+For+Chain+G'>AC7</scene> and <scene name='pdbsite=AC8:Hem+Binding+Site+For+Chain+H'>AC8</scene> | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2veb|2VEB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vee OCA], [http://www.ebi.ac.uk/pdbsum/2vee PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vee RCSB]</span> | ||
}} | }} | ||
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[[Category: Saito, J A.]] | [[Category: Saito, J A.]] | ||
[[Category: Thijs, L.]] | [[Category: Thijs, L.]] | ||
| - | [[Category: HEM]] | ||
[[Category: archaea protein]] | [[Category: archaea protein]] | ||
[[Category: hemoprotein structure]] | [[Category: hemoprotein structure]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:11:13 2008'' |
Revision as of 02:11, 31 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Related: | 2VEB
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PROTOGLOBIN FROM METHANOSARCINA ACETIVORANS C2A
Overview
The structural adaptability of the globin fold has been highlighted by the recent discovery of the 2-on-2 haemoglobins, of neuroglobin and cytoglobin. Protoglobin from Methanosarcina acetivorans C2A-a strictly anaerobic methanogenic Archaea-is, to the best of our knowledge, the latest entry adding new variability and functional complexity to the haemoglobin (Hb) superfamily. Here, we report the 1.3 A crystal structure of oxygenated M. acetivorans protoglobin, together with the first insight into its ligand-binding properties. We show that, contrary to all known globins, protoglobin-specific loops and an amino-terminal extension completely bury the haem within the protein matrix. Access of O(2), CO and NO to the haem is granted by the protoglobin-specific apolar tunnels reaching the haem distal site from locations at the B/G and B/E helix interfaces. Functionally, M. acetivorans dimeric protoglobin shows a selectivity ratio for O(2)/CO binding to the haem that favours O(2) ligation and anticooperativity in ligand binding. Both properties are exceptional within the Hb superfamily.
About this Structure
2VEE is a Single protein structure of sequence from Methanosarcina acetivorans. Full crystallographic information is available from OCA.
Reference
Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity., Nardini M, Pesce A, Thijs L, Saito JA, Dewilde S, Alam M, Ascenzi P, Coletta M, Ciaccio C, Moens L, Bolognesi M, EMBO Rep. 2008 Feb;9(2):157-63. Epub 2008 Jan 11. PMID:18188182
Page seeded by OCA on Mon Mar 31 05:11:13 2008
Categories: Methanosarcina acetivorans | Single protein | Alam, M. | Ascenzi, P. | Bolognesi, M. | Ciaccio, C. | Coletta, M. | Dewilde, S. | Moens, L. | Nardini, M. | Pesce, A. | Saito, J A. | Thijs, L. | Archaea protein | Hemoprotein structure | Methanogenesis | Protein matrix tunnel | Protoglobin | Transport protein
