3bk7
From Proteopedia
| Line 3: | Line 3: | ||
{{Structure | {{Structure | ||
|PDB= 3bk7 |SIZE=350|CAPTION= <scene name='initialview01'>3bk7</scene>, resolution 2.800Å | |PDB= 3bk7 |SIZE=350|CAPTION= <scene name='initialview01'>3bk7</scene>, resolution 2.800Å | ||
| - | |SITE= | + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+594'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+A+595'>AC2</scene>, <scene name='pdbsite=AC3:Sf4+Binding+Site+For+Residue+A+596'>AC3</scene>, <scene name='pdbsite=AC4:Sf4+Binding+Site+For+Residue+A+597'>AC4</scene>, <scene name='pdbsite=AC5:Adp+Binding+Site+For+Residue+A+598'>AC5</scene> and <scene name='pdbsite=AC6:Adp+Binding+Site+For+Residue+A+599'>AC6</scene> |
|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| - | |DOMAIN= | + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd03236 ABC_RNaseL_inhibitor_domain1], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd03237 ABC_RNaseL_inhibitor_domain2], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1245 COG1245]</span> |
|RELATEDENTRY=[[1yqt|1yqt]] | |RELATEDENTRY=[[1yqt|1yqt]] | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bk7 OCA], [http://www.ebi.ac.uk/pdbsum/3bk7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bk7 RCSB]</span> | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bk7 OCA], [http://www.ebi.ac.uk/pdbsum/3bk7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bk7 RCSB]</span> | ||
| Line 14: | Line 14: | ||
'''Structure of the complete ABCE1/RNAase-L Inhibitor protein from Pyrococcus abysii''' | '''Structure of the complete ABCE1/RNAase-L Inhibitor protein from Pyrococcus abysii''' | ||
| + | |||
| + | ==Overview== | ||
| + | The ATP binding cassette enzyme ABCE1 (also known as RNase-L (ribonuclease L) inhibitor, Pixie, and HP68), one of the evolutionary most sequence-conserved enzymes, functions in translation initiation, ribosome biogenesis, and human immunodeficiency virus capsid assembly. However, its structural mechanism and biochemical role in these processes have not been revealed. We determined the crystal structure of Pyrococcus abyssi ABCE1 in complex with Mg(2+) and ADP to 2.8A resolution. ABCE1 consists of four structural domains. Two nucleotide binding domains are arranged in a head-to-tail orientation by a hinge domain, suggesting that these domains undergo the characteristic tweezers-like powerstroke of ABC enzymes. In contrast to all other known ABC enzymes, ABCE1 has a N-terminal iron-sulfur-cluster (FeS) domain. The FeS domain contains two [4Fe-4S] clusters and is structurally highly related to bacterial-type ferredoxins. However, one cluster is coordinated by an unusual CX(4)CX(3/4)C triad. Surprisingly, intimate interactions of the FeS domain with the adenine and ribose binding Y-loop on nucleotide binding domain 1 suggest a linkage between FeS domain function and ATP-induced conformational control of the ABC tandem cassette. The structure substantially expands the functional architecture of ABC enzymes and raises the possibility that ABCE1 is a chemomechanical engine linked to a redox process. | ||
==About this Structure== | ==About this Structure== | ||
3BK7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK7 OCA]. | 3BK7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK7 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | X-ray Structure of the Complete ABC Enzyme ABCE1 from Pyrococcus abyssi., Karcher A, Schele A, Hopfner KP, J Biol Chem. 2008 Mar 21;283(12):7962-71. Epub 2007 Dec 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18160405 18160405] | ||
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 34: | ||
[[Category: nucleotide-binding]] | [[Category: nucleotide-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:32:42 2008'' |
Revision as of 08:32, 2 April 2008
| |||||||
| , resolution 2.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , , | ||||||
| Domains: | ABC_RNaseL_inhibitor_domain1, ABC_RNaseL_inhibitor_domain2, COG1245 | ||||||
| Related: | 1yqt
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the complete ABCE1/RNAase-L Inhibitor protein from Pyrococcus abysii
Overview
The ATP binding cassette enzyme ABCE1 (also known as RNase-L (ribonuclease L) inhibitor, Pixie, and HP68), one of the evolutionary most sequence-conserved enzymes, functions in translation initiation, ribosome biogenesis, and human immunodeficiency virus capsid assembly. However, its structural mechanism and biochemical role in these processes have not been revealed. We determined the crystal structure of Pyrococcus abyssi ABCE1 in complex with Mg(2+) and ADP to 2.8A resolution. ABCE1 consists of four structural domains. Two nucleotide binding domains are arranged in a head-to-tail orientation by a hinge domain, suggesting that these domains undergo the characteristic tweezers-like powerstroke of ABC enzymes. In contrast to all other known ABC enzymes, ABCE1 has a N-terminal iron-sulfur-cluster (FeS) domain. The FeS domain contains two [4Fe-4S] clusters and is structurally highly related to bacterial-type ferredoxins. However, one cluster is coordinated by an unusual CX(4)CX(3/4)C triad. Surprisingly, intimate interactions of the FeS domain with the adenine and ribose binding Y-loop on nucleotide binding domain 1 suggest a linkage between FeS domain function and ATP-induced conformational control of the ABC tandem cassette. The structure substantially expands the functional architecture of ABC enzymes and raises the possibility that ABCE1 is a chemomechanical engine linked to a redox process.
About this Structure
3BK7 is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
X-ray Structure of the Complete ABC Enzyme ABCE1 from Pyrococcus abyssi., Karcher A, Schele A, Hopfner KP, J Biol Chem. 2008 Mar 21;283(12):7962-71. Epub 2007 Dec 26. PMID:18160405
Page seeded by OCA on Wed Apr 2 11:32:42 2008
