User:Karl Oberholser/Sandbox2
From Proteopedia
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HMfB Seq: MELPIAPIGR IIKDAGAERV SDDARITLAK ILEEMGRDIA SEAIKLARHA GRKTIKAEDI ELAVRRFKK <br> | HMfB Seq: MELPIAPIGR IIKDAGAERV SDDARITLAK ILEEMGRDIA SEAIKLARHA GRKTIKAEDI ELAVRRFKK <br> | ||
| - | Comparing the above sequences one can see that an important difference is that A has a | + | Comparing the above sequences one can see that an important difference is that A has a glycine at position 2 which is lacking in B. In addition to that deletion, there are a number of substitutions which creates differences in the sequence of the two peptides. As a consequence of this similarity of primary structure, as shown in the two applets below, the tertiary structures of both peptides are quite similar. |
<applet load='1hta' size='400' frame='true' align='left' caption='HMfA, PDB ID:1hta' name='1' /> | <applet load='1hta' size='400' frame='true' align='left' caption='HMfA, PDB ID:1hta' name='1' /> | ||
| - | <applet load='1a7w' size='400' frame='true' align='right' caption='HMfB, PDB ID: 1a7w' name='2' /> | + | <applet load='1a7w' size='400' frame='true' align='right' caption='HMfB, PDB ID: 1a7w' name='2' scene='User:Karl_Oberholser/Sandbox2/1a7w_first/1' /> |
| - | Also the location of the nonpolar residues within the tertiary structure are similarly located <scene name='User:Karl_Oberholser/Sandbox2/Nonpolar_1hta/1' target='1'>HMfA</scene>, <scene name='User:Karl_Oberholser/Sandbox2/Nonpolar_1a7w/ | + | Also the location of the nonpolar residues within the tertiary structure are similarly located <scene name='User:Karl_Oberholser/Sandbox2/Nonpolar_1hta/1' target='1'>HMfA</scene>, <scene name='User:Karl_Oberholser/Sandbox2/Nonpolar_1a7w/2' target='2'>HMfB</scene>. |
{{STRUCTURE_1b67 | PDB=1b67 | SCENE=}} | {{STRUCTURE_1b67 | PDB=1b67 | SCENE=}} | ||
Revision as of 14:13, 20 January 2010
Histones HMfA and HMfB from Methanothermus fervidus
"The hyperthermophilic archaeon Methanothermus fervidus contains two small basic proteins, HMfA (68 amino acid residues) and HMfB (69 residues)that share a common ancestry with the eukaryal nucleosome core histones H2A, H2B, H3, and H4. HMfA and HMfB have sequences that differ at 11 locations, they have different structural stabilities, and the complexes that they form with DNA have different electrophoretic mobilities." [1]
Comparison of Structures
HMfA Seq: MGELPIAPIG RIIKNAGAER VSDDARIALA KVLEEMGEEI ASEAVKLAKH AGRKTIKAED IELARKMFK
HMfB Seq: MELPIAPIGR IIKDAGAERV SDDARITLAK ILEEMGRDIA SEAIKLARHA GRKTIKAEDI ELAVRRFKK
Comparing the above sequences one can see that an important difference is that A has a glycine at position 2 which is lacking in B. In addition to that deletion, there are a number of substitutions which creates differences in the sequence of the two peptides. As a consequence of this similarity of primary structure, as shown in the two applets below, the tertiary structures of both peptides are quite similar.
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Also the location of the nonpolar residues within the tertiary structure are similarly located , .
Template:STRUCTURE 1b67 The orthorombic form of PDB:1B67 is shown in the default scene as a dimer structure
Notes and References
- ↑ From abstract of K. Decanniere, A. M. Babu, K. Sandman, J. N. Reeve, U. Heinemann Crystal Structure of Recombinant Histones HMfA and HMfB from the Hyperthermophilic Methanothermus fervidus. J. Mol. Biol., 303, 35-47, 2000
