1urd

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[[Image:1urd.gif|left|200px]]<br /><applet load="1urd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1urd.gif|left|200px]]
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caption="1urd, resolution 1.53&Aring;" />
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'''X-RAY STRUCTURES OF THE MALTOSE-MALTODEXTRIN BINDING PROTEIN OF THE THERMOACIDOPHILIC BACTERIUM ALICYCLOBACILLUS ACIDOCALDARIUS PROVIDE INSIGHT INTO ACID STABILITY OF PROTEINS'''<br />
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{{Structure
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|PDB= 1urd |SIZE=350|CAPTION= <scene name='initialview01'>1urd</scene>, resolution 1.53&Aring;
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|SITE= <scene name='pdbsite=AC1:Mlr+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''X-RAY STRUCTURES OF THE MALTOSE-MALTODEXTRIN BINDING PROTEIN OF THE THERMOACIDOPHILIC BACTERIUM ALICYCLOBACILLUS ACIDOCALDARIUS PROVIDE INSIGHT INTO ACID STABILITY OF PROTEINS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1URD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius] with <scene name='pdbligand=MLR:'>MLR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Mlr+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URD OCA].
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1URD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URD OCA].
==Reference==
==Reference==
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X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins., Schafer K, Magnusson U, Scheffel F, Schiefner A, Sandgren MO, Diederichs K, Welte W, Hulsmann A, Schneider E, Mowbray SL, J Mol Biol. 2004 Jan 2;335(1):261-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14659755 14659755]
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X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins., Schafer K, Magnusson U, Scheffel F, Schiefner A, Sandgren MO, Diederichs K, Welte W, Hulsmann A, Schneider E, Mowbray SL, J Mol Biol. 2004 Jan 2;335(1):261-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14659755 14659755]
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermophile]]
[[Category: thermophile]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:44 2008''

Revision as of 12:35, 20 March 2008

Image:1urd.gif


PDB ID 1urd

Drag the structure with the mouse to rotate
, resolution 1.53Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



X-RAY STRUCTURES OF THE MALTOSE-MALTODEXTRIN BINDING PROTEIN OF THE THERMOACIDOPHILIC BACTERIUM ALICYCLOBACILLUS ACIDOCALDARIUS PROVIDE INSIGHT INTO ACID STABILITY OF PROTEINS


Overview

Maltose-binding proteins act as primary receptors in bacterial transport and chemotaxis systems. We report here crystal structures of the thermoacidostable maltose-binding protein from Alicyclobacillus acidocaldarius, and explore its modes of binding to maltose and maltotriose. Further, comparison with the structures of related proteins from Escherichia coli (a mesophile), and two hyperthermophiles (Pyrococcus furiosus and Thermococcus litoralis) allows an investigation of the basis of thermo- and acidostability in this family of proteins.The thermoacidophilic protein has fewer charged residues than the other three structures, which is compensated by an increase in the number of polar residues. Although the content of acidic and basic residues is approximately equal, more basic residues are exposed on its surface whereas most acidic residues are buried in the interior. As a consequence, this protein has a highly positive surface charge. Fewer salt bridges are buried than in the other MBP structures, but the number exposed on its surface does not appear to be unusual. These features appear to be correlated with the acidostability of the A. acidocaldarius protein rather than its thermostability.An analysis of cavities within the proteins shows that the extremophile proteins are more closely packed than the mesophilic one. Proline content is slightly higher in the hyperthermophiles and thermoacidophiles than in mesophiles, and this amino acid is more common at the second position of beta-turns, properties that are also probably related to thermostability. Secondary structural content does not vary greatly in the different structures, and so is not a contributing factor.

About this Structure

1URD is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.

Reference

X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins., Schafer K, Magnusson U, Scheffel F, Schiefner A, Sandgren MO, Diederichs K, Welte W, Hulsmann A, Schneider E, Mowbray SL, J Mol Biol. 2004 Jan 2;335(1):261-74. PMID:14659755

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